Biomolecules

Carbohydrates
Monosaccharides- Glucose, Fructose, Galactose
Disaccharides- Sucrose, Lactose, Maltose
Polysaccharides- Starch, Glycogen, Cellulose

*insoluble in water and do not taste sweet

Hydroxyl groups make carbohydrates polar
Lipids
make 18-25% of body mass
few polar covalent bonds because of hydrogen oxygen ratio
insoluble in polar solvents such as water- hydrophobic
composed of primarily hydrogen and carbon atoms
non-polar covalent bonds
Fatty Acids
-simplest lipid
-used to synthesize triglycerides and phospholipids
-carboxly group and hydrocarbon chain
-either saturated or unsaturated
Saturated fatty acid- contains single covalent bonds; each carbon atom of
the hydrocarbon chain is saturated with hydrogen atoms
Unsaturated fatty acid- contains one or more double covalent bonds; not
completely saturated with hydrogen atoms; has a kink or bend at site of
covalent bond
*Classes of Lipids
Triglycerides
Phospholipids
Steroids
Triglycerides
Most plentiful lipid in body
Made of single glycerol molecule and three fatty acid molecules
Fatty acid chains make triglycerides hydrophobic
Phospholipids
In third position a phosphate group links a small charged group that
usually contains nitrogen to the backbones, making this portion polar
and form with hydrogen bonds with water molecules
The two fatty acids are nonpolar and can interact with other lipids

 Amphipathic- have both polar and nonpolar parts

Make up a lot of the membrane that surrounds each cell
Steroids
Have four rings of carbon atoms
Commonly encountered steroids are cholesterol, estrogen,
testosterone, cortisol, bile salts, and vitamin D= sterols because they
have at least one hydroxyl group
Proteins
Made up of 20 amino acids
There are 9 essential that we must consume in diet that the body does
not make enough of
11 non-essential that the cells can make
Responsible for the structure of body tissues
Ex) Enzymes are proteins that speed up most biochemical reactions
large molecules that contain carbon, hydrogen, oxygen, and nitrogen,
some contain sulfur
Amino Acids
-monomer of protein
each has a Hydrogen atom: amino group- R group- Carboxyl group
The R group is what makes every amino acid different
The covalent bond joining each pair of amino acid is a peptide bond
Peptides- generally 2-50 amino acids
Proteins- greater than 50 amino acids
When a peptide bond occurs a molecule of water is removed make this
a dehydration synthesis reactions
Breaking a peptide bond occurs during digestions of dietary proteins a
hydrolysis reaction occurs
Levels of Structural Organization in Proteins
Four levels
Primary- amino acids are linked by a covalent peptide bonds to form a
polypeptide chain- like a pearl necklace
Genetically determined, and changes can have serious consequences
Sickle cell disease- a nonpolar amino acid (valine) replaces a polar
amino acid (glutamate) through two mutations in the oxygen-carrying
protein hemoglobin. This change diminishes hemoglobins water
solubility therefore producing crystals inside red blood cells
Secondary- protein is the repeated twisting or folding of neighboring amino
acids in the polypeptide chain
Alpha helixes and beta pleated sheets
Stabilized in hydrogen bonds

Tertiary structure- three dimensional shape of polypeptide chain

Disulfide bridges
Hydrogen bonds
Ionic bonds
Hydrophobic interactions
Van Der Waals Forces
All help determine the folding patterns
Quaternary structure- formation of proteins with more than one polypeptide
chain
Fibrous proteins- insoluble in water and their polypeptide chains form long
strands that are parallel to each other
Collagen- strengthens bones, ligaments, and tendons
Elastin-provides stretch in skin, blood vessels, and lung tissue
Keratin-hair and nail structures, waterproofs skin
Dystrophine-reinforces muscle cells
Globular proteins- more or less soluble in water and their polypeptide
chains are spherical in shape
Metabolic functions
Enzymes which function as catalysts
Antibodies, complement proteins
Hemoglobin-transports oxygen
Lipoproteins-transport lipids and cholesterol
Membrane proteins- transport substances into and out of cells
Some hormones
Enzymes
Protein and non protein portion
Names of enzymes usually end in ase
They are highly specific- each enzyme binds to only specific substrates
which is the reactant molecules on which the enzyme reacts
They are very efficient- can catalyze reactions that are more rapid
Subject to a variety of cellular controls- their rate of synthesis and their
concentration at any given time are under the control of a cells genes
Nucleic Acids- DNA and RNA
Names because they were the first discovered in the nuclei of cells,
contain carbon, hydrogen, oxygen, nitrogen, and phosphorous
Polymers of nucleotides
DNA; deoxyribonucleic acid- forms the inherited genetic material inside
each human cell; gene- is a segment of a DNA molecule

RNA-ribonucleic acid- relays instruction from the genes to guide each

cells synthesis of protein from amino acids

DNA
Carbohydrate= deoxyribose Chain of repeating monomers called nucleotides- each have three
parts: Base, Sugar, Phosphate group
1) Nitrogen base- Purines: Adenine and Guanine; Pyrimidines: Cytosine
and Thymine
2) Pentose Sugar
3) Phosphate group
Double stranded
Helix
Law of Complimentary Base- A-T (A-U), C-G
A with T, G with C
RNA

Sugar-Ribose
Bases: Purines: Adenine and Guanine; Pyrimidines: Cytosine and Uracil
Single stranded
Messenger RNA, Ribosomal RNA, and Transfer RNA
Rule: A with U, and G with C

Adenosine Triphosphate
ATP
Is the energy currency of living systems
Transfers energy liberated in exergonic catabolic reactions to power
cellular activities that require energy
Muscular contractions, movement of chromosomes during cell division,
transport substances around cell membranes, synthesis of larger
molecule from smaller ones