PROTEINS

Proteins
Proteins do the nitty-gritty jobs of every living cell. Proteins are made of long strings of individual building blocks known as amino acids.

Amino acids contain an amino group, a carboxyl group, a carbon and a unique R group

3.2.2

Identify amino acids ... from diagrams showing their structure.

Polar R groups make the amino acid hydrophilic

Non-polar R groups make the amino acid hydrophobic

Ionic R groups make the amino acid hydrophilic

7.5.3

Explain the significance of polar and non-polar amino acids.

There are 20 commonly occurring amino acids that are found in proteins
alanine - ala - A arginine - arg - R *** asparagine - asn - N aspartic acid - asp - D cysteine - cys - C glutamine - gln - Q glutamic acid - glu - E glycine - gly - G histidine - his - H *** isoleucine - ile - I
leucine - leu - L lysine - lys - K methionine - met - M phenylalanine - phe - F proline - pro - P serine - ser - S threonine - thr - T tryptophan - trp - W tyrosine - tyr - Y valine - val - V

Essential Amino Acids are those that must be ingested in the diet (our body cant make them)

Peptide Bonds join amino acids

Its a condensation reaction (meaning that H20 is released when the bond is formed).

Two amino acids form a DI-PEPTIDE

POLYPEPTIDES are formed from more than two amino acids bonded together

Outline the role of condensation and hydrolysis in the relationships between amino acids and polypeptides. 7.4.5 Draw and label a diagram showing the structure of a peptide bond between two amino acids.
3.2.5

Proteins have four levels of organization

Primary structure is the amino acid sequence

The amino acid sequence is coded for by DNA and is unique for each kind of protein

The amino acid sequence determines how the polypeptide will fold into its 3D shape

Even a slight change in the amino acid sequence can cause the protein to malfunction

For example, mis-formed hemoglobin causes sickle cell disease

Proteins have four levels of organization

Secondary structure results from hydrogen bonding between the oxygen of one amino acid and the hydrogen of another

The alpha helix is a coiled secondary structure due to a hydrogen bond every fourth amino acid

The beta pleated sheet is formed by hydrogen bonds between parallel parts of the protein

A single polypeptide may have portions with both types of secondary structure

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Proteins have four levels of organization

Tertiary structure depends on the interactions among the R group side chains

Types of interactions
Hydrophobic interactions: amino acids with nonpolar side chains cluster in the core of the protein, out of contact with water

= charged

= hydrophobic

Types of interactions
Hydrogen bonds between polar side chains

Types of interactions
Ionic bonds between positively and negatively charged side chains

Types of interactions
Disulfide bridge (strong covalent bonds) between sulfur atoms in the amino acid cysteine

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Proteins have four levels of organization

Quaternary structure results from interactions among separate polypeptide chains.

For example, hemoglobin is composed of 4 polypeptide chains

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Proteins have four levels of organization

The folding of proteins is aided by other proteins, called chaperones

Act as temporary braces as proteins fold into their final conformation Research into chaperones is a area of research in biology

7.5.1

Explain the four levels of protein structure, indicating the significance of each level.

Denaturation results in disruption of the secondary, tertiary, or quaternary structure of the protein

Denaturation may be due to changes in pH, temperature or various chemicals

Protein function is lost during denaturation, which is often irreversible

3.6.4
Define denaturation.

Folded proteins are placed into two general categories

GLOBULAR and FIBROUS PROTEINS

 Scleroproteins, or fibrous proteins,

constitute one of the two main classes of proteins, alongside Globular proteins

Fibrous proteins have polypeptide chains organized in long fibers or sheets

Water insoluble Very tough physically, may be stretchy

Functions of fibrous proteins

Structural proteins function in support
Insects and spiders use silk fibers to make cocoons and webs Collagen and elastin are used in animal tendons and ligaments Keratin is the protein in hairs, horns and feathers

COLLAGEN
Collagen is a group of naturally occurring proteins found in animals, especially in the flesh and connective tissues of vertebrates. It is the main component of connective tissue, and is the most abundant protein in mammals, making up about 25% to 35% of the wholebody protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendon, ligament and skin, and is also abundant in cornea, cartilage, bone, blood vessels, the gut, and intervertebral disc. The fibroblast is the most common cell which creates collagen.

 Collagen is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins such as enzymes. Tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside certain cells.

 Collagen has great tensile strength, and is the main component of cartilage, ligaments, tendons, bone and skin. Along with soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. It strengthens blood vessels and plays a role in tissue development. It is present in the cornea and lens of the eye in crystalline form.

KERATIN
Keratin is a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human skin It is also the key structural component of hair and nails.

Functions of fibrous proteins

Contractile proteins function in movement
Actin and myosin contract to create the cleavage furrow and to move muscles Contractile proteins move cilia and flagella

Globular protein

 Globular proteins, or spheroproteins, constitute

one of the two main protein classes, with the other classes being the fibrous. Globular proteins are spherical ("globe-like") proteins that are somewhat water-soluble, unlike the fibrous protein.

Globular proteins have their chains folded into compact, rounded shapes
Easily water soluble

Functions of globular proteins

Storage proteins function in the storage of amino acids
albumin is the protein in egg whites Casein is the protein in milk, source of amino acids for baby mammals

Functions of globular proteins

Transport proteins function in the movement of other substances
Hemoglobin, the iron containing protein in blood, transport oxygen from lungs to other parts of the body (C3032H4816O872N780S9Fe4) Membrane transport proteins such as channels for potassium and water

Functions of globular proteins

Hormone proteins function as cellular messenger molecules that help maintain homeostasis
Insulin: sends message allow sugar into cells (when blood glucose levels are high, cells will transport glucose into the cells for use or storage) Glucagon: sends message we need more sugar in the blood (when blood glucose is too low, cells will release glucose)

Functions of globular proteins

Receptor proteins allow cells to respond to chemical stimuli
Growth factor receptors initiate the signal transduction pathway when a growth hormone attaches

Functions of globular proteins

Cholesterol receptors on the cell membrane allow LDL to be endocytosed into the cell

Functions of globular proteins

Protective proteins function as protection against disease
Antibodies combat bacteria and viruses

Functions of globular proteins

Enzymes speed up chemical reactions
Amylase and other digestive enzymes hydrolyze polymers in food Catalase converts hydrogen peroxide H2O2 into water and oxygen gas during cellular respiration