Introduction

Think back to what you ate for lunch. Did any of your lunch items have a “Nutrition Facts” label
on the back of them? If so, and if you had a look at the food's protein, carbohydrate, or fat
content, you may already be familiar with several types of large biological molecules we’ll
discuss here. If you’re wondering what something as weird-sounding as a “large biological
molecule” is doing in your food, the answer is that it’s providing you with the building blocks
you need to maintain your body – because your body is also made of large biological molecules!
Just as you can be thought of as an assortment of atoms or a walking, talking bag of water, you
can also be viewed as a collection of four major types of large biological molecules:
carbohydrates (such as sugars), lipids (such as fats), proteins, and nucleic acids (such as DNA
and RNA). That’s not to say that these are the only molecules in your body, but rather, that your
most important large molecules can be divided into these groups. Together, the four groups of
large biological molecules make up the majority of the dry weight of a cell. (Water, a small
molecule, makes up the majority of the wet weight).
Large biological molecules perform a wide range of jobs in an organism. Some carbohydrates
store fuel for future energy needs, and some lipids are key structural components of cell
membranes. Nucleic acids store and transfer hereditary information, much of which provides
instructions for making proteins. Proteins themselves have perhaps the broadest range of
functions: some provide structural support, but many are like little machines that carry out
specific jobs in a cell, such as catalyzing metabolic reactions or receiving and transmitting
signals.
We’ll look in greater detail at carbohydrates, lipids, nucleic acids, and proteins a few articles
down the road. Here, we’ll look a bit more at the key chemical reactions that build up and break
down these molecules.
Monomers and polymers
Most large biological molecules are polymers, long chains made up of repeating molecular
subunits, or building blocks, called monomers. If you think of a monomer as being like a bead,
then you can think of a polymer as being like a necklace, a series of beads strung together.
Carbohydrates, nucleic acids, and proteins are often found as long polymers in nature. Because
of their polymeric nature and their large (sometimes huge!) size, they are classified
as macromolecules, big (macro-) molecules made through the joining of smaller subunits.
Lipids are not usually polymers and are smaller than the other three, so they are not considered
macromolecules by some sources^{1,2}1,2start superscript, 1, comma, 2, end superscript.
However, many other sources use the term “macromolecule” more loosely, as a general name for
the four types of large biological molecules^{3,4}3,4start superscript, 3, comma, 4, end
superscript. This is just a naming difference, so don’t get too hung up on it. Just remember that
lipids are one of the four main types of large biological molecules, but that they don’t generally
form polymers.
Dehydration synthesis
How do you build polymers from monomers? Large biological molecules often assemble
via dehydration synthesis reactions, in which one monomer forms a covalent bond to another
monomer (or growing chain of monomers), releasing a water molecule in the process. You can
remember what happens by the name of the reaction: dehydration, for the loss of the water
molecule, and synthesis, for the formation of a new bond.

Dehydration synthesis reaction between two molecules of glucose, forming a molecule of

maltose with the release of a water molecule.
In the dehydration synthesis reaction above, two molecules of the sugar glucose (monomers)
combine to form a single molecule of the sugar maltose. One of the glucose molecules loses an
H, the other loses an OH group, and a water molecule is released as a new covalent bond forms
between the two glucose molecules. As additional monomers join by the same process, the chain
can get longer and longer and form a polymer.
Even though polymers are made out of repeating monomer units, there is lots of room for variety
in their shape and composition. Carbohydrates, nucleic acids, and proteins can all contain
multiple different types of monomers, and their composition and sequence is important to their
function. For instance, there are four types of nucleotide monomers in your DNA, as well as
twenty types of amino acid monomers commonly found in the proteins of your body. Even a
single type of monomer may form different polymers with different properties. For example,
starch, glycogen, and cellulose are all carbohydratesmade up of glucose monomers, but they
have different bonding and branching patterns.
Hydrolysis
How do polymers turn back into monomers (for instance, when the body needs to recycle one
molecule to build a different one)? Polymers are broken down into monomers

via hydrolysis reactions, in which a bond is broken, or lysed, by addition of a water molecule.
During a hydrolysis reaction, a molecule composed of multiple subunits is split in two: one of
the new molecules gains a hydrogen atom, while the other gains a hydroxyl (-OH) group, both of
which are donated by water. This is the reverse of a dehydration synthesis reaction, and it
releases a monomer that can be used in building a new polymer. For example, in the hydrolysis

reaction below, a water molecule splits maltose to release two glucose monomers. This reaction
is the reverse of the dehydration synthesis reaction shown above.

Hydrolysis of maltose, in which a molecule of maltose combines with a molecule of water,

resulting in the formation of two glucose monomers.
Dehydration synthesis reactions build molecules up and generally require energy, while
hydrolysis reactions break molecules down and generally release energy. Carbohydrates,
proteins, and nucleic acids are built up and broken down via these types of reactions, although
the monomers involved are different in each case. (In a cell, nucleic acids actually aren't
polymerized via dehydration synthesis; we’ll examine how they're assembled in the article
on nucleic acids. Dehydration synthesis reactions are also involved in the assembly of certain
types of lipids, even though the lipids are not polymers^33start superscript, 3, end superscript.
In the body, enzymes catalyze, or speed up, both the dehydration synthesis and hydrolysis
reactions. Enzymes involved in breaking bonds are often given names that end with -ase: for
instance, the maltase enzyme breaks down maltose, lipases break down lipids, and peptidases
break down proteins (also known as polypeptides, as we’ll see in the article on proteins). As food
travels through your digestive system – in fact, from the moment it hits your saliva – it is being
worked over by enzymes like these. The enzymes break down large biological molecules,
releasing the smaller building blocks that can be readily absorbed and used by the body.
Carbohydrates
Overview of carbohydrates, including structure and properties of monosaccharides,
disaccharides, and polysaccharides.
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Introduction

What’s in a spud? Besides water, which makes up most of the potato’s weight, there’s a little fat,
a little protein…and a whole lot of carbohydrate (about 37 grams in a medium potato).

Some of that carbohydrate is in the form of sugars. These provide the potato, and the person
eating the potato, with a ready fuel source. A bit more of the potato's carbohydrate is in the form
of fiber, including cellulose polymers that give structure to the potato’s cell walls. Most of the
carbohydrate, though, is in the form of starch, long chains of linked glucose molecules that are a
storage form of fuel. When you eat French fries, potato chips, or a baked potato with all the
fixings, enzymes in your digestive tract get to work on the long glucose chains, breaking them
down into smaller sugars that your cells can use.

Carbohydrates are biological molecules made of carbon, hydrogen, and oxygen in a ratio of
roughly one carbon atom (\text CCC) to one water molecule (\text H_2\text OH2OH, start
subscript, 2, end subscript, O). This composition gives carbohydrates their name: they are made
up of carbon (carbo-) plus water (-hydrate). Carbohydrate chains come in different lengths, and
biologically important carbohydrates belong to three categories: monosaccharides, disaccharides,
and polysaccharides. In this article, we’ll learn more about each type of carbohydrates, as well as
the essential energetic and structural roles they play in humans and other organisms.

Monosaccharides

Monosaccharides (mono- = “one”; sacchar- = “sugar”) are simple sugars, the most common of
which is glucose. Monosaccharides have a formula of (\text {CH}_2\text O)_n(CH2O)nleft
 parenthesis, C, H, start subscript, 2, end subscript, O, right parenthesis, start subscript, n, end
subscript, and they typically contain three to seven carbon atoms.
[How is that formula different from carbohydrates in general?]

\text CC\text H_2\text OH, start subscript, 2, end subscript, O

\text CC\text H_2\text OH, start subscript, 2, end subscript, O

\text HH\text OO\text CC

Most of the oxygen atoms in monosaccharides are found in hydroxyl (\text {OH}OHO, H)
groups, but one of them is part of a carbonyl (\text C=\text OC=OC, equals, O) group. The
position of the carbonyl (\text C=\text OC=OC, equals, O) group can be used to categorize the
sugars:

 If the sugar has an aldehyde group, meaning that the carbonyl C is the last one in the chain, it is
known as an aldose.
 If the carbonyl C is internal to the chain, so that there are other carbons on both sides of it, it
forms a ketone group and the sugar is called a ketose.
Sugars are also named according to their number of carbons: some of the most common types are
trioses (three carbons), pentoses (five carbons), and hexoses (six carbons).

Structures of monosaccharides. By carbonyl position: glyceraldehyde (aldose), dihydroxyacetone

(ketose). By number of carbons: glyceraldehyde (triose), ribose (pentose), and glucose (hexose).
Structure of aldehyde: carbonyl bonded to a H on one side and to an R group (carbon-containing
group) on the other. Structure of ketone: carbonyl bonded to R and R' groups (carbon-containing
groups) on both sides.

Image modified from OpenStax Biology.

Glucose and its isomers

One important monosaccharide is glucose, a six-carbon sugar with the formula \text C_6\text
H_{12}\text O_6C6H12O6C, start subscript, 6, end subscript, H, start subscript, 12, end
subscript, O, start subscript, 6, end subscript. Other common monosaccharides include galactose
(which forms part of lactose, the sugar found in milk) and fructose (found in fruit).

Glucose, galactose, and fructose have the same chemical formula (\text C_6\text H_{12}\text
O_6C6H12O6C, start subscript, 6, end subscript, H, start subscript, 12, end subscript, O, start
subscript, 6, end subscript), but they differ in the organization of their atoms, making
them isomers of one another. Fructose is a structural isomer of glucose and galactose, meaning
that its atoms are actually bonded together in a different order.

Glucose and galactose are stereoisomers (have atoms bonded together in the same order, but
differently arranged in space). They differ in their stereochemistry at carbon 4. Fructose is a
structural isomer of glucose and galactose (has the same atoms, but bonded together in a different
order).
Image modified from OpenStax Biology.

Glucose and galactose are stereoisomers of each other: their atoms are bonded together in the
same order, but they have a different 3D organization of atoms around one of their asymmetric
carbons. You can see this in the diagram as a switch in the orientation of the hydroxyl
(\text{OH}OHO, H) group, marked in red. This small difference is enough for enzymes to tell
glucose and galactose apart, picking just one of the sugars to take part in chemical
reactions^11start superscript, 1, end superscript.

Ring forms of sugars

You may have noticed that the sugars we’ve looked at so far are linear molecules (straight
chains). That may seem odd because sugars are often drawn as rings. As it turns out both are
correct: many five- and six-carbon sugars can exist either as a linear chain or in one or more
ring-shaped forms.

These forms exist in equilibrium with each other, but equilibrium strongly favors the ring forms
(particularly in aqueous, or water-based, solution). For instance, in solution, glucose’s main
configuration is a six-membered ring. Over 99% of glucose is typically found in this
form^33start superscript, 3, end superscript.

Even when glucose is in a six-membered ring, it can occur in two different forms with different
properties. During ring formation, the \text OOO from the carbonyl, which is converted to a
hydroxyl group, will be trapped either “above” the ring (on the same side as
the \text{CH}_2\text{OH}CH2OHC, H, start subscript, 2, end subscript, O, H group) or “below”
the ring (on the opposite side from this group). When the hydroxyl is down, glucose is said to be
in its alpha (α) form, and when it’s up, glucose is said to be in its beta (β) form.
 Linear and ring forms of glucose. The linear form can convert into either the alpha or the beta
ring form, with the two forms differing in the position of the hydroxyl group derived from the
carbonyl of the linear form. If the hydroxyl is up (on the same side as the CH_22start subscript,
2, end subscriptOH group), then the molecule is beta glucose, while if it is down (on the opposite
side), then the molecule is alpha glucose.

Also pictured ring forms of ribose and fructose. Unlike the six-membered glucose rings, these
rings are five-membered.
Image modified from OpenStax Biology.
Disaccharides

Disaccharides (di- = “two”) form when two monosaccharides join together via a dehydration
reaction, also known as a condensation reaction or dehydration synthesis. In this process, the
hydroxyl group of one monosaccharide combines with the hydrogen of another, releasing a
molecule of water and forming a covalent bond known as a glycosidic linkage.

For instance, the diagram below shows glucose and fructose monomers combining via a
dehydration reaction to form sucrose, a disaccharide we know as table sugar. (The reaction also
releases a water molecule, not pictured.)

Formation of a 1-2 glycosidic linkage between glucose and fructose via dehydration synthesis.
Image credit: OpenStax Biology.

In some cases, it’s important to know which carbons on the two sugar rings are connected by a
glycosidic bond. Each carbon atom in a monosaccharide is given a number, starting with the
terminal carbon closest to the carbonyl group (when the sugar is in its linear form). This
numbering is shown for glucose and fructose, above. In a sucrose molecule, the 111 carbon of
glucose is connected to the 222 carbon of fructose, so this bond is called a 111-222 glycosidic
linkage.

Common disaccharides include lactose, maltose, and sucrose. Lactose is a disaccharide

consisting of glucose and galactose and is found naturally in milk. Many people can't digest
lactose as adults, resulting in lactose intolerance (which you or your friends may be all too
familiar with). Maltose, or malt sugar, is a disaccharide made up of two glucose molecules. The
most common disaccharide is sucrose (table sugar), which is made of glucose and fructose.
 Common disaccharides: maltose, lactose, and sucrose
Image credit: OpenStax Biology.

Polysaccharides
 A long chain of monosaccharides linked by glycosidic bonds is known as
a polysaccharide (poly- = “many”). The chain may be branched or unbranched and may contain
different types of monosaccharides. The molecular weight of a polysaccharide can be quite high,
reaching 100,100,100, comma000000000 daltons or more if enough monomers are joined.
Starch, glycogen, cellulose, and chitin are some major examples of polysaccharides important in
living organisms.

Storage polysaccharides

Starch is the stored form of sugars in plants and is made up of a mixture of two polysaccharides,
amylose and amylopectin (both polymers of glucose). Plants are able to synthesize glucose using
light energy gathered in photosynthesis, and the excess glucose, beyond the plant’s immediate
energy needs, is stored as starch in different plant parts, including roots and seeds. The starch in
the seeds provides food for the embryo as it germinates and can also serve as a food source for
humans and animals, who will break it down into glucose monomers using digestive enzymes.

In starch, the glucose monomers are in the α form (with the hydroxyl group of
carbon 111 sticking down below the ring), and they are connected primarily by 111-
444 glycosidic linkages (i.e., linkages in which carbon atoms 111 and 444 of the two monomers
form a glycosidic bond).

 Amylose consists entirely of unbranched chains of glucose monomers connected by 111-

444 linkages.
 Amylopectin is a branched polysaccharide. Although most of its monomers are connected
by 111-444 linkages, additional 111-666 linkages occur periodically and result in branch points.
Because of the way the subunits are joined, the glucose chains in amylose and amylopectin
typically have a helical structure, as shown in the diagram below.
 Top: amylose has a linear structure and is made of glucose monomers connected by 1-4
glycosidic linkages. Bottom: amylopectin has a branching structure. It is mostly made of glucose
molecules connected by 1-4 glycosidic linkages, but has glucose molecules connected by 1-6
linkages at the branch points.
Image credit: OpenStax Biology.
That’s great for plants, but what about us? Glycogen is the storage form of glucose in humans
and other vertebrates. Like starch, glycogen is a polymer of glucose monomers, and it is even
more highly branched than amylopectin.

Glycogen is usually stored in liver and muscle cells. Whenever blood glucose levels decrease,
glycogen is broken down via hydrolysis to release glucose monomers that cells can absorb and
use.

Structural polysaccharides

Although energy storage is one important role for polysaccharides, they are also crucial for
another purpose: providing structure. Cellulose, for example, is a major component of plant cell
walls, which are rigid structures that enclose the cells (and help make lettuce and other veggies
crunchy). Wood and paper are mostly made of cellulose, and cellulose itself is made up of
unbranched chains of glucose monomers linked by 111-444 glycosidic bonds.

Cellulose fibers and molecular structure of cellulose. Cellulose is made of glucose monomers in
the beta form, and this results in a chain where every other monomer is flipped upside down
relative to its neighbors.
Image modified from OpenStax Biology.

Unlike amylose, cellulose is made of glucose monomers in their β form, and this gives it very
different properties. As shown in the figure above, every other glucose monomer in the chain is
flipped over in relation to its neighbors, and this results in long, straight, non-helical chains of
cellulose. These chains cluster together to form parallel bundles that are held together by
hydrogen bonds between hydroxyl groups^{4,5}4,5start superscript, 4, comma, 5, end
superscript. This gives cellulose its rigidity and high tensile strength, which are important to
plant cells.

The β glycosidic linkages in cellulose can't be broken by human digestive enzymes, so humans
are not able to digest cellulose. (That’s not to say that cellulose isn’t found in our diets, it just
passes through us as undigested, insoluble fiber.) However, some herbivores, such as cows,
koalas, buffalos, and horses, have specialized microbes that help them process cellulose. These
microbes live in the digestive tract and break cellulose down into glucose monomers that can be
used by the animal. Wood-chewing termites also break down cellulose with the help of
microorganisms that live in their guts.

Image of a bee. The bee's exoskeleton (hard outer shell) contains chitin, which is made out of
modified glucose units that have a nitrogenous functional group attached to them.
Image credit: Louise Docker.

Cellulose is specific to plants, but polysaccharides also play an important structural role in non-
plant species. For instance, arthropods (such as insects and crustaceans) have a hard external
skeleton, called the exoskeleton, which protects their softer internal body parts. This exoskeleton
is made of the macromolecule chitin, which resembles cellulose but is made out of modified
glucose units that bear a nitrogen-containing functional group. Chitin is also a major component
of the cell walls of fungi, which are neither animals nor plants but form a kingdom of their own.

Lipids
Overview of lipids, covering fats and oils, saturated and unsaturated fats, triglycerides
(triacylglycerols), phospholipids, and steroids.
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Introduction

We sometimes talk about fat as if it were a malevolent substance bent on our dietary destruction.
In reality, fats are elegant little molecules, each one made of three long hydrocarbon tails
attached to a little coathanger-like molecule called glycerol. Like the other large biological
molecules, they play essential roles in the biology of humans and other organisms. (Also, many
recent dietary studies see sugar as causing a lot more health problems than fat!)

Fats are just one type of lipid, a category of molecules united by their inability to mix well with
water. Lipids tend to be hydrophobic, nonpolar, and made up mostly of hydrocarbon chains,
though there are some variations on this, which we'll explore below. The different varieties of
lipids have different structures, and correspondingly diverse roles in organisms. For instance,
lipids store energy, provide insulation, make up cell membranes, form water-repellent layers on
leaves, and provide building blocks for hormones like testosterone.

Here, we’ll look in greater detail at some of the most important types of lipids, including fats and
oils, waxes, phospholipids, and steroids.

Fats and oils

A fat molecule consists of two kinds of parts: a glycerol backbone and three fatty acid tails.
Glycerol is a small organic molecule with three hydroxyl (OH) groups, while a fatty acid consists
of a long hydrocarbon chain attached to a carboxyl group. A typical fatty acid contains 12–18
carbons, though some may have as few as 4 or as many as 36.

To make a fat molecule, the hydroxyl groups on the glycerol backbone react with the carboxyl
groups of fatty acids in a dehydration synthesis reaction. This yields a fat molecule with three
fatty acid tails bound to the glycerol backbone via ester linkages (linkages containing an oxygen
atom next to a carbonyl, or C=O, group). Triglycerides may contain three identical fatty acid
tails, or three different fatty acid tails (with different lengths or patterns of double bonds).
 Synthesis of a tryacylglycerol molecule from a glycerol backbone and three fatty acid chains,
with the release of three molecules of water.
Image modified from OpenStax Biology.

Fat molecules are also called triacylglycerols, or, in bloodwork done by your
doctor, triglycerides. In the human body, triglycerides are primarily stored in specialized fat
 cells, called adipocytes, which make up a tissue known as adipose tissue^11start superscript, 1,
end superscript. While many fatty acids are found in fat molecules, some are also free in the
body, and they are considered a type of lipid in their own right.

Saturated and unsaturated fatty acids

As shown in the example above, the three fatty acid tails of a triglyceride need not be identical to
each other. Fatty acid chains may differ in length, as well as in their degree of unsaturation.

 If there are only single bonds between neighboring carbons in the hydrocarbon chain, a fatty acid
is said to be saturated. (The thing that fatty acids are saturated with is hydrogen; in a saturated
fat, as many hydrogen atoms as possible are attached to the carbon skeleton.)
 When the hydrocarbon chain has a double bond, the fatty acid is said to be unsaturated, as it
now has fewer hydrogens. If there is just one double bond in a fatty acid, it’s monounsaturated,
while if there are multiple double bonds, it’s polyunsaturated.
The double bonds in unsaturated fatty acids, like other types of double bonds, can exist in either
a cis or a trans configuration. In the cis configuration, the two hydrogens associated with the
bond are on the same side, while in a transconfiguration, they are on opposite sides (see below).
A cis double bond generates a kink or bend in the fatty acid, a feature that has important
consequences for the behavior of fats.
 Saturated fatty acid example: stearic acid (straight shape). Unsaturated fatty acid examples: cis
oleic acid (cisdouble bond, bent chain), trans oleic acid (transdouble bond, straight chain).
Image credit: OpenStax Biology.

Saturated fatty acids tails are straight, so fat molecules with fully saturated tails can pack tightly
against one another. This tight packing results in fats that are solid at room temperature (have a
relatively high melting point). For instance, most of the fat in butter is saturated fat^22start
superscript, 2, end superscript.

In contrast, cis-unsaturated fatty acid tails are bent due to the cis double bond. This makes it hard
for fat molecules with one or more cis-unsaturated fatty acid tails to pack tightly. So, fats with
unsaturated tails tend to be liquid at room temperature (have a relatively low melting point) –
they are what we commonly call oils. For instance, olive oil is mostly made up of unsaturated
fats^22start superscript, 2, end superscript.

Trans fats

At this point, you may be noticing that I’ve left something out: I didn’t say anything about
unsaturated fats with trans double bonds in their fatty acid tails, or trans fats. Trans fats are rare
in nature, but are readily produced in an industrial procedure called partial hydrogenation.

In this process, hydrogen gas is passed through oils (made mostly of cis-unsaturated fats),
converting some – but not all – of the double bonds to single bonds. The goal of partial
hydrogenation is to give the oils some of the desirable properties of saturated fats, such as
solidity at room temperature, but an unintended consequence is that some of the cis double bonds
change configuration and become trans double bonds^33start superscript, 3, end
superscript. Trans-unsaturated fatty acids can pack more tightly and are more likely to be solid at
room temperature. Some types of shortening, for example, contain a high fraction
of trans fats^33start superscript, 3, end superscript.

Partial hydrogenation and trans fats might seem like a good way to get a butter-like substance at
oil-like prices. Unfortunately, trans fats have turned out to have very negative effects on human
health. Because of a strong link between trans fats and coronary heart disease, the U.S. Food and
Drug Administration (FDA) recently issued a ban on trans fats in foods, with a three-year
deadline for companies to remove trans fats from their products^44start superscript, 4, end
superscript.

Omega fatty acids

Another class of fatty acids that deserves mention includes the omega-3 and omega-6 fatty
acids. There are different types of omega-3 and omega-6 fatty acids, but all of them are made
from two basic precursor forms: alpha-linolenic acid (ALA) for omega-3s and linoleic acid (LA)
for omega-6s.

The human body needs these molecules (and their derivatives), but can't synthesize either ALA
or LA itself^55start superscript, 5, end superscript. Accordingly, ALA and LA are classified
as essential fatty acids and must be obtained from a person’s diet. Some fish, such as salmon,
and some seeds, such as chia and flax, are good sources of omega-3 fatty acids.

Omega-3 and omega-6 fatty acids have at least two cis-unsaturated bonds, which gives them a
curved shape. ALA, shown below, is quite bent but isn’t the most extreme example – DHA, an
omega-3 fatty acid made from ALA by the formation of additional double bonds, has six cis-
unsaturated bonds and is curled up almost in a circle!
[What makes a fatty acid omega-3 or omega-6?]

Image of alpha-linoleic acid (ALA), showing its curled shape due to its three cisdouble bonds.
Image credit: OpenStax Biology.

Omega-3 and omega-6 fatty acids play a number of different roles in the body. They are
precursors (starting material) for the synthesis of a number of important signaling molecules,
including ones that regulate inflammation and mood. Omega-3 fatty acids in particular may
reduce the risk of sudden death from heart attacks, decrease triglycerides in the blood, lower
blood pressure, and prevent the formation of blood clots.
Role of fats

Fats have received a lot of bad publicity, and it’s true that eating large amounts of fried foods
and other “fatty” foods can lead to weight gain and cause health problems. However, fats are
essential to the body and have a number of important functions.

For instance, many vitamins are fat-soluble, meaning that they must be associated with fat
molecules in order to be effectively absorbed by the body. Fats also provide an efficient way to
store energy over long time periods, since they contain over twice as much energy per gram as
carbohydrates, and they additionally provide insulation for the body.

Like all the other large biological molecules, fats in the right amounts are necessary to keep your
body (and the bodies of other organisms) functioning correctly.

Waxes

Waxes are another biologically important category of lipids. Wax covers the feathers of some
aquatic birds and the leaf surfaces of some plants, where its hydrophobic (water-repelling)
properties prevent water from sticking to, or soaking into, the surface. This is why water beads
up on the leaves of many plants, and why birds don’t get soaked through when it rains.
 Image of shiny leaf surface covered with wax.
Image credit: OpenStax Biology.

Structurally speaking, waxes typically contain long fatty acid chains connected to alcohols by
ester linkages, although waxes produced by plants often have plain hydrocarbons mixed in as
well^66start superscript, 6, end superscript.

Phospholipids

What keeps the watery goo (cytosol) inside of your cells from spilling out? Cells are surrounded
by a structure called the plasma membrane, which serves as a barrier between the inside of the
cell and its surroundings.

Specialized lipids called phospholipids are major components of the plasma membrane. Like
fats, they are typically composed of fatty acid chains attached to a backbone of glycerol. Instead
having three fatty acid tails, however, phospholipids generally have just two, and the third
carbon of the glycerol backbone is occupied by a modified phosphate group. Different
phospholipids have different modifiers on the phosphate group, with choline (a nitrogen-
containing compound) and serine (an amino acid) being common examples. Different modifiers
give phospholipids different properties and roles in a cell.

Structure of a phospholipid, showing hydrophobic fatty acid tails and hydrophilic head (including
ester linkages, glycerol backbone, phosphate group, and attached R group on phosphate group).
A bilayered membrane consisting of phospholipids arranged in two layers, with their heads
pointing out and their tails sandwiched in the middle, is also shown.
Image modified from OpenStax Biology.

A phospholipid is an amphipathic molecule, meaning it has a hydrophobic part and a

hydrophilic part. The fatty acid chains are hydrophobic and do not interact with water, whereas
the phosphate-containing group is hydrophilic (because of its charge) and interacts readily with
water. In a membrane, phospholipids are arranged into a structure called a bilayer, with their
phosphate heads facing the water and their tails pointing towards the inside (above). This
organization prevents the hydrophobic tails from coming into contact with the water, making it a
low-energy, stable arrangement.
If a drop of phospholipids is placed in water, it may spontaneously form a sphere-shaped
structure known as a micelle, in which the hydrophilic phosphate heads face the outside and the
fatty acids face the interior of this structure. Formation of micelle is an energetically favored
because it sequesters the hydrophobic fatty acid tails, allowing the hydrophilic phosphate head
group to instead interact with the surrounding water^{7,8}7,8start superscript, 7, comma, 8, end
superscript.
[More details]

^{7,8}start superscript, 7, comma, 8, end superscript

Steroids

Steroids are another class of lipid molecules, identifiable by their structure of four fused rings.
Although they do not resemble the other lipids structurally, steroids are included in lipid
category because they are also hydrophobic and insoluble in water. All steroids have four linked
carbon rings and several of them, like cholesterol, also have a short tail. Many steroids also have
an –OH functional group attached at a particular site, as shown for cholesterol below; such
steroids are also classified as alcohols, and are thus called sterols.
Examples of steroids: cholesterol and cortisol. Both have the characteristic structure of four fused
hydrocarbon rings.
Image credit: OpenStax Biology.
[Stereochemistry of cholesterol]
Cholesterol, the most common steroid, is mainly synthesized in the liver and is the precursor to
many steroid hormones. These include the sex hormones testosterone and estradiol, which are
secreted by the gonads (testes and ovaries). Cholesterol also serves as the starting material for
other important molecules in the body, including vitamin D and bile acids, which aid in the
digestion and absorption of fats from dietary sources. It’s also a key component of cell
membranes, altering their fluidity and dynamics.

Of course, cholesterol is also found in the bloodstream, and blood levels of cholesterol are what
we often hear about at the doctor’s office or in news reports. Cholesterol in the blood can have
both protective effects (in its high-density, or HDL, form) and negative effects (in its low-
density, or LDL, form) on cardiovascular health.

Introduction
Nucleic acids, and DNA in particular, are key macromolecules for the
continuity of life. DNA bears the hereditary information that’s passed on
from parents to children, providing instructions for how (and when) to make
the many proteins needed to build and maintain functioning cells, tissues, and
organisms.

How DNA carries this information, and how it is put into action by cells and
organisms, is complex, fascinating, and fairly mind-blowing, and we’ll
explore it in more detail in the section on molecular biology. Here, we’ll just
take a quick look at nucleic acids from the macromolecule perspective.

Roles of DNA and RNA in cells

Nucleic acids, macromolecules made out of units called nucleotides, come in
two naturally occurring varieties: deoxyribonucleic acid (DNA)
and ribonucleic acid (RNA). DNA is the genetic material found in living
organisms, all the way from single-celled bacteria to multicellular mammals
like you and me. Some viruses use RNA, not DNA, as their genetic material,
but aren’t technically considered to be alive (since they cannot reproduce
without help from a host).

DNA in cells
In eukaryotes, such as plants and animals, DNA is found in the nucleus, a
specialized, membrane-bound vault in the cell, as well as in certain other
types of organelles (such as mitochondria and the chloroplasts of plants). In
prokaryotes, such as bacteria, the DNA is not enclosed in a membranous
envelope, although it's located in a specialized cell region called
the nucleoid.

In eukaryotes, DNA is typically broken up into a number of very long, linear

pieces called chromosomes, while in prokaryotes such as bacteria,
chromosomes are much smaller and often circular (ring-shaped). A
chromosome may contain tens of thousands of genes, each providing
instructions on how to make a particular product needed by the cell.

From DNA to RNA to proteins

Many genes encode protein products, meaning that they specify the sequence
of amino acids used to build a particular protein. Before this information can
be used for protein synthesis, however, an RNA copy (transcript) of the gene
must first be made. This type of RNA is called a messenger RNA (mRNA),
as it serves as a messenger between DNA and the ribosomes, molecular
machines that read mRNA sequences and use them to build proteins. This
progression from DNA to RNA to protein is called the “central dogma” of
molecular biology.

Importantly, not all genes encode protein products. For instance, some genes
specify ribosomal RNAs (rRNAs), which serve as structural components of
ribosomes, or transfer RNAs (tRNAs), cloverleaf-shaped RNA molecules
that bring amino acids to the ribosome for protein synthesis. Still other RNA
molecules, such as tiny microRNAs (miRNAs), act as regulators of other
genes, and new types of non-protein-coding RNAs are being discovered all
the time.

Nucleotides
DNA and RNA are polymers (in the case of DNA, often very long polymers),
and are made up of monomers known as nucleotides. When these monomers
combine, the resulting chain is called a polynucleotide (poly- = "many").

Each nucleotide is made up of three parts: a nitrogen-containing ring

structure called a nitrogenous base, a five-carbon sugar, and at least one
phosphate group. The sugar molecule has a central position in the nucleotide,
with the base attached to one of its carbons and the phosphate group (or
groups) attached to another. Let’s look at each part of a nucleotide in turn.

Image of the components of DNA and RNA, including the sugar

(deoxyribose or ribose), phosphate group, and nitrogenous base. Bases
include the pyrimidine bases (cytosine, thymine in DNA, and uracil in RNA,
one ring) and the purine bases (adenine and guanine, two rings). The
phosphate group is attached to the 5' carbon. The 2' carbon bears a hydroxyl
group in ribose, but no hydroxyl (just hydrogen) in deoxyribose.
_Image modified from "Nucleic acids: Figure 1," by OpenStax College, Biology (CC BY 3.0)._

Nitrogenous bases
The nitrogenous bases of nucleotides are organic (carbon-based) molecules
made up of nitrogen-containing ring structures.
[Why is it called a base?]

^+start superscript, plus, end superscript

Each nucleotide in DNA contains one of four possible nitrogenous bases:

adenine (A), guanine (G) cytosine (C), and thymine (T). Adenine and
guanine are purines, meaning that their structures contain two fused carbon-
nitrogen rings. Cytosine and thymine, in contrast, are pyrimidines and have a
single carbon-nitrogen ring. RNA nucleotides may also bear adenine, guanine
and cytosine bases, but instead of thymine they have another pyrimidine base
called uracil (U). As shown in the figure above, each base has a unique
structure, with its own set of functional groups attached to the ring structure.

In molecular biology shorthand, the nitrogenous bases are often just referred
to by their one-letter symbols, A, T, G, C, and U. DNA contains A, T, G, and
C, while RNA contains A, U, G, and C (that is, U is swapped in for T).

Sugars
In addition to having slightly different sets of bases, DNA and RNA
nucleotides also have slightly different sugars. The five-carbon sugar in DNA
is called deoxyribose, while in RNA, the sugar is ribose. These two are very
similar in structure, with just one difference: the second carbon of ribose
bears a hydroxyl group, while the equivalent carbon of deoxyribose has a
hydrogen instead. The carbon atoms of a nucleotide’s sugar molecule are
numbered as 1′, 2′, 3′, 4′, and 5′ (1′ is read as “one prime”), as shown in the
figure above. In a nucleotide, the sugar occupies a central position, with the
base attached to its 1′ carbon and the phosphate group (or groups) attached to
its 5′ carbon.

Phosphate
Nucleotides may have a single phosphate group, or a chain of up to three
phosphate groups, attached to the 5’ carbon of the sugar. Some chemistry
sources use the term “nucleotide” only for the single-phosphate case, but in
molecular biology, the broader definition is generally accepted^11start
superscript, 1, end superscript

In a cell, a nucleotide about to be added to the end of a polynucleotide chain

will bear a series of three phosphate groups. When the nucleotide joins the
growing DNA or RNA chain, it loses two phosphate groups. So, in a chain of
DNA or RNA, each nucleotide has just one phosphate group.

Polynucleotide chains
A consequence of the structure of nucleotides is that a polynucleotide chain
has directionality – that is, it has two ends that are different from each other.
At the 5’ end, or beginning, of the chain, the 5’ phosphate group of the first
nucleotide in the chain sticks out. At the other end, called the 3’ end, the 3’
hydroxyl of the last nucleotide added to the chain is exposed. DNA sequences
are usually written in the 5' to 3' direction, meaning that the nucleotide at the
5' end comes first and the nucleotide at the 3' end comes last.

As new nucleotides are added to a strand of DNA or RNA, the strand grows
at its 3’ end, with the 5′ phosphate of an incoming nucleotide attaching to the
hydroxyl group at the 3’ end of the chain. This makes a chain with each sugar
joined to its neighbors by a set of bonds called a phosphodiester linkage.

Properties of DNA
Deoxyribonucleic acid, or DNA, chains are typically found in a double helix,
a structure in which two matching (complementary) chains are stuck together,
as shown in the diagram at left. The sugars and phosphates lie on the outside
of the helix, forming the backbone of the DNA; this portion of the molecule
is sometimes called the sugar-phosphate backbone. The nitrogenous bases
extend into the interior, like the steps of a staircase, in pairs; the bases of a
pair are bound to each other by hydrogen bonds.
 Structural model of a DNA double helix.
Image credit: Jerome Walker/Dennis Myts.

The two strands of the helix run in opposite directions, meaning that the 5′
end of one strand is paired up with the 3′ end of its matching strand. (This is
referred to as antiparallel orientation and is important for the copying of
DNA.)

So, can any two bases decide to get together and form a pair in the double
helix? The answer is a definite no. Because of the sizes and functional groups
of the bases, base pairing is highly specific: A can only pair with T, and G
can only pair with C, as shown below. This means that the two strands of a
DNA double helix have a very predictable relationship to each other.

For instance, if you know that the sequence of one strand is 5’-AATTGGCC-
3’, the complementary strand must have the sequence 3’-TTAACCGG-5’.
This allows each base to match up with its partner:

5'-AATTGGCC-3' 3'-TTAACCGG-5'

These two strands are complementary, with each base in one sticking to its
partner on the other. The A-T pairs are connected by two hydrogen bonds,
while the G-C pairs are connected by three hydrogen bonds.

When two DNA sequences match in this way, such that they can stick to each
other in an antiparallel fashion and form a helix, they are said to
be complementary.
 Hydrogen bonding between complementary bases holds DNA strands
together in a double helix of antiparallel strands. Thymine forms two
hydrogen bonds with adenine, and guanine forms three hydrogen bonds with
cytosine.
Image modified from OpenStax Biology.

Properties of RNA
Ribonucleic acid (RNA), unlike DNA, is usually single-stranded. A
nucleotide in an RNA chain will contain ribose (the five-carbon sugar), one
of the four nitrogenous bases (A, U, G, or C), and a phosphate group. Here,
we'll take a look at four major types of RNA: messenger RNA (mRNA),
ribosomal RNA (rRNA), transfer RNA (tRNA), and regulatory RNAs.

Messenger RNA (mRNA)

Messenger RNA (mRNA) is an intermediate between a protein-coding gene
and its protein product. If a cell needs to make a particular protein, the gene
encoding the protein will be turned “on,” meaning an RNA-polymerizing
enzyme will come and make an RNA copy, or transcript, of the gene’s DNA
sequence. The transcript carries the same information as the DNA sequence
of its gene. However, in the RNA molecule, the base T is replaced with U.
For instance, if a DNA coding strand has the sequence 5’-AATTGCGC-3’,
the sequence of the corresponding RNA will be 5’-AAUUGCGC-3’.

Once an mRNA has been produced, it will associate with a ribosome, a

molecular machine that specializes in assembling proteins out of amino acids.
The ribosome uses the information in the mRNA to make a protein of a
specific sequence, “reading out” the mRNA’s nucleotides in groups of three
(called codons) and adding a particular amino acid for each codon.

Image of a ribosome (made of proteins and rRNA) bound to an mRNA, with

tRNAs bringing amino acids to be added to the growing chain. The tRNA that
binds, and thus the amino acid that's added, at a given moment is determined
by the sequence of the mRNA that is being "read" at that time.
Image credit: OpenStax Biology.

Ribosomal RNA (rRNA) and transfer RNA (tRNA)

Ribosomal RNA (rRNA) is a major component of ribosomes, where it helps
mRNA bind in the right spot so its sequence information can be read out.
Some rRNAs also act as enzymes, meaning that they help accelerate
(catalyze) chemical reactions – in this case, the formation of bonds that link
amino acids to form a protein. RNAs that act as enzymes are known
as ribozymes.

Transfer RNAs (tRNAs) are also involved in protein synthesis, but their job
is to act as carriers – to bring amino acids to the ribosome, ensuring that the
amino acid added to the chain is the one specified by the mRNA. Transfer
RNAs consist of a single strand of RNA, but this strand has complementary
segments that stick together to make double-stranded regions. This base-
pairing creates a complex 3D structure important to the function of the
molecule.

Structure of a tRNA. The overall molecule has a shape somewhat like an L.

Image modified from Protein Data Bank (work of the U.S. government).

Regulatory RNA (miRNAs and siRNAs)

Some types of non-coding RNAs (RNAs that do not encode proteins) help
regulate the expression of other genes. Such RNAs may be called regulatory
RNAs. For example, microRNAs (miRNAs) and small interfering
RNAs siRNAsare small regulatory RNA molecules about 22 nucleotides
long. They bind to specific mRNA molecules (with partly or fully
complementary sequences) and reduce their stability or interfere with their
translation, providing a way for the cell to decrease or fine-tune levels of
these mRNAs.

These are just some examples out of many types of noncoding and regulatory
RNAs. Scientists are still discovering new varieties of noncoding RNA.
[More about regulatory RNAs]

^2start superscript, 2, end superscript

Summary: Features of DNA and RNA

DNA RNA

Involved in protein synthesis and gene

Repository of regulation; carrier of genetic information
Function genetic information in some viruses

Sugar Deoxyribose Ribose

Structure Double helix Usually single-stranded

Bases C, T, A, G C, U, A, G

Orders of protein structure

Orders of protein structure: primary, secondary, tertiary, and quaternary. Alpha helix and beta
pleated sheet.
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Introduction
Have you ever wondered why egg whites go from clear to opaque when you
fry an egg? If so, this section is for you!

Egg whites contain large amounts of proteins called albumins, and the
albumins normally have a specific 3D shape, thanks to bonds formed
between different amino acids in the protein. Heating causes these bonds to
break and exposes hydrophobic (water-hating) amino acids usually kept on
the inside of the protein^{1,2}1,2start superscript, 1, comma, 2, end
superscript. The hydrophobic amino acids, trying to get away from the water
surrounding them in the egg white, will stick to one another, forming a
protein network that gives the egg white structure while turning it white and
opaque. Ta-da! Thank you, protein denaturation, for another delicious
breakfast.

As we mentioned in the last article on proteins and amino acids, the shape of
a protein is very important to its function. To understand how a protein gets
its final shape or conformation, we need to understand the four levels of
protein structure: primary, secondary, tertiary, and quaternary.

Primary structure
The simplest level of protein structure, primary structure, is simply the
sequence of amino acids in a polypeptide chain. For example, the hormone
insulin has two polypeptide chains, A and B, shown in diagram below. (The
insulin molecule shown here is cow insulin, although its structure is similar to
that of human insulin.) Each chain has its own set of amino acids, assembled
in a particular order. For instance, the sequence of the A chain starts with
glycine at the N-terminus and ends with asparagine at the C-terminus, and is
different from the sequence of the B chain.
[What's up with those S-S bonds?]

Image of insulin. Insulin consists of an A chain and a B chain. They are

connected to one another by disulfide bonds (sulfur-sulfur bonds between
cysteines). The A chain also contains an internal disulfide bond. The amino
acids that make up each chain of insulin are represented as connected circles,
each with the three-letter abbreviation of the amino acid's name.
image credit: OpenStax Biology.

The sequence of a protein is determined by the DNA of the gene that encodes
the protein (or that encodes a portion of the protein, for multi-subunit
proteins). A change in the gene's DNA sequence may lead to a change in the
amino acid sequence of the protein. Even changing just one amino acid in a
protein’s sequence can affect the protein’s overall structure and function.

For instance, a single amino acid change is associated with sickle cell
anemia, an inherited disease that affects red blood cells. In sickle cell anemia,
one of the polypeptide chains that make up hemoglobin, the protein that
carries oxygen in the blood, has a slight sequence change. The glutamate that
is normally the seventh amino acid of the hemoglobin β chain (one of two
types of protein chains that make up hemoglobin) is replaced by a valine.
This substitution is shown for a fragment of the β chain in the diagram below.

Image of normal and sickle cell mutant hemoglobin chains, showing

substitution of valine for glutamate in the sickle cell version.
Image modified from OpenStax Biology.

What is most remarkable to consider is that a hemoglobin molecule is made

up of two α chains and two β chains, each consisting of about 150 amino
acids, for a total of about 600 amino acids in the whole protein. The
difference between a normal hemoglobin molecule and a sickle cell molecule
is just 2 amino acids out of the approximately 600.

A person whose body makes only sickle cell hemoglobin will suffer
symptoms of sickle cell anemia. These occur because the glutamate-to-valine
amino acid change makes the hemoglobin molecules assemble into long
fibers. The fibers distort disc-shaped red blood cells into crescent shapes.
Examples of “sickled” cells can be seen mixed with normal, disc-like cells in
the blood sample below.

Image credit: OpenStax Biology modification of work by Ed Uthman; scale-bar data from Matt Russell.

The sickled cells get stuck as they try to pass through blood vessels. The
stuck cells impair blood flow and can cause serious health problems for
people with sickle cell anemia, including breathlessness, dizziness,
headaches, and abdominal pain.

Secondary structure
The next level of protein structure, secondary structure, refers to local
folded structures that form within a polypeptide due to interactions between
atoms of the backbone. (The backbone just refers to the polypeptide chain
apart from the R groups – so all we mean here is that secondary structure
does not involve R group atoms.) The most common types of secondary
structures are the α helix and the β pleated sheet. Both structures are held in
shape by hydrogen bonds, which form between the carbonyl O of one amino
acid and the amino H of another.

Images showing hydrogen bonding patterns in beta pleated sheets and alpha
helices.
Image credit: OpenStax Biology.

In an α helix, the carbonyl (C=O) of one amino acid is hydrogen bonded to

the amino H (N-H) of an amino acid that is four down the chain. (E.g., the
carbonyl of amino acid 1 would form a hydrogen bond to the N-H of amino
acid 5.) This pattern of bonding pulls the polypeptide chain into a helical
structure that resembles a curled ribbon, with each turn of the helix
containing 3.6 amino acids. The R groups of the amino acids stick outward
from the α helix, where they are free to interact^33start superscript, 3, end
superscript.

In a β pleated sheet, two or more segments of a polypeptide chain line up

next to each other, forming a sheet-like structure held together by hydrogen
bonds. The hydrogen bonds form between carbonyl and amino groups of
backbone, while the R groups extend above and below the plane of the
sheet^33start superscript, 3, end superscript. The strands of a β pleated sheet
may be parallel, pointing in the same direction (meaning that their N- and C-
termini match up), or antiparallel, pointing in opposite directions (meaning
that the N-terminus of one strand is positioned next to the C-terminus of the
other).

Certain amino acids are more or less likely to be found in α-helices or β

pleated sheets. For instance, the amino acid proline is sometimes called a
“helix breaker” because its unusual R group (which bonds to the amino group
to form a ring) creates a bend in the chain and is not compatible with helix
formation^44start superscript, 4, end superscript. Proline is typically found in
bends, unstructured regions between secondary structures. Similarly, amino
acids such as tryptophan, tyrosine, and phenylalanine, which have large ring
structures in their R groups, are often found in β pleated sheets, perhaps
because the β pleated sheet structure provides plenty of space for the side
chains^44start superscript, 4, end superscript.

Many proteins contain both α helices and β pleated sheets, though some
contain just one type of secondary structure (or do not form either type).

Tertiary structure
The overall three-dimensional structure of a polypeptide is called its tertiary
structure. The tertiary structure is primarily due to interactions between the
R groups of the amino acids that make up the protein.

R group interactions that contribute to tertiary structure include hydrogen

bonding, ionic bonding, dipole-dipole interactions, and London dispersion
forces – basically, the whole gamut of non-covalent bonds. For example, R
groups with like charges repel one another, while those with opposite charges
can form an ionic bond. Similarly, polar R groups can form hydrogen bonds
and other dipole-dipole interactions. Also important to tertiary structure
are hydrophobic interactions, in which amino acids with nonpolar,
hydrophobic R groups cluster together on the inside of the protein, leaving
hydrophilic amino acids on the outside to interact with surrounding water
molecules.

Finally, there’s one special type of covalent bond that can contribute to
tertiary structure: the disulfide bond. Disulfide bonds, covalent linkages
between the sulfur-containing side chains of cysteines, are much stronger
than the other types of bonds that contribute to tertiary structure. They act
like molecular "safety pins," keeping parts of the polypeptide firmly attached
to one another.
 Image of a hypothetical polypeptide chain, depicting different types of side
chain interactions that can contribute to tertiary structure. These include
hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridge
formation.
Image modified from OpenStax Biology.

Quaternary structure
Many proteins are made up of a single polypeptide chain and have only three
levels of structure (the ones we’ve just discussed). However, some proteins
are made up of multiple polypeptide chains, also known as subunits. When
these subunits come together, they give the protein its quaternary structure.

We’ve already encountered one example of a protein with quaternary

structure: hemoglobin. As mentioned earlier, hemoglobin carries oxygen in
the blood and is made up of four subunits, two each of the α and β types.
Another example is DNA polymerase, an enzyme that synthesizes new
strands of DNA and is composed of ten subunits^55start superscript, 5, end
superscript.

In general, the same types of interactions that contribute to tertiary structure

(mostly weak interactions, such as hydrogen bonding and London dispersion
forces) also hold the subunits together to give quaternary structure.
 Flowchart depicting the four orders of protein structure.
Image modified from OpenStax Biology's modification of work by the National Human Genome Research
Institute.
Denaturation and protein folding
Each protein has its own unique shape. If the temperature or pH of a protein's
environment is changed, or if it is exposed to chemicals, these interactions
may be disrupted, causing the protein to lose its three-dimensional structure
and turn back into an unstructured string of amino acids. When a protein
loses its higher-order structure, but not its primary sequence, it is said to
be denatured. Denatured proteins are usually non-functional.

For some proteins, denaturation can be reversed. Since the primary structure
of the polypeptide is still intact (the amino acids haven’t split up), it may be
able to re-fold into its functional form if it's returned to its normal
environment. Other times, however, denaturation is permanent. One example
of irreversible protein denaturation is when an egg is fried. The albumin
protein in the liquid egg white becomes opaque and solid as it is denatured by
the heat of the stove, and will not return to its original, raw-egg state even
when cooled down.

Researchers have found that some proteins can re-fold after denaturation
even when they are alone in a test tube. Since these proteins can go from
unstructured to folded all by themselves, their amino acid sequences must
contain all the information needed for folding. However, not all proteins are
able to pull off this trick, and how proteins normally fold in a cell appears to
be more complicated. Many proteins don’t fold by themselves, but instead get
assistance from chaperone proteins (chaperonins).