The structures of collagen and keratin

Biology
kadita sookdeo 10/7/13 Lower6

Collagen
Collagen is an extracellular, naturally occurring group of fibrous proteins found in animals. They are found in the flesh and is the main component of connective tissues is vertebrates. Collagen provides toughness to skin, bone, cartilage, tendons, teeth, ligaments and muscles. Collagen has several levels of organisation and is the most abundant protein in mammals; making up about 25% to 30% of the wholebody protein content. Collagen is also found in structures ranging from the body wall of sea anemones to the egg cases of dogfish.

The structure of collagen.

Collagen is made up of about 1000 amino acids that form a polypeptide chain in a stretched out helix. Glycine which is the smallest amino acid, occurs almost every third amino acid in each polypeptide chain. Glycine has the smallest R-group (-H) hence its small size allows the three strands to lie close together to form a tight coil. Any other amino acid would be too large. Three helices are wound together to form a triple helix (Tropocollagen)/ a collagen molecule. The three strands are held together by hydrogen bonds. Each complete triple helix join with another triple helix, running parallel to it, by covalent bonds to form a network of fibres that form Fibrils. The ends of triple helices do not occur at the

same time within the fibrils so there are no lines of weakness where the fibrils may break. Fibrils join to form bundles called Fibres. This arrangement makes collagen suitable for structures such as tendons that have high tensile strength and resist pulling forces.

The human Achilles tendon (a tendon of the posterior leg), which is almost all collagen fibres, can with stand a pulling force of 300N mm of the cross sectional area.

A comparison between the structures and functions of collagen and cellulose.

Cellulose is a poly saccharide and collagen is a protein, but both have similar structural features and functions.

CELLULOSE

COLLAGEN

COLLAGEN Collagen is a protein. Collagen is a polymer made of amino acids linked by polypeptide bonds. Collagen sub units consists of three polypeptide chains. Many different monomer units are used to make collagen. (Examples: glycine, alanine) Collagen is a structural protein in animal. (Examples: connective tissues, bones, teeth, tendons, ligaments etc.)

CELLULOSE Cellulose is a polysaccharide. Cellulose is a polymer of beta glucose residues linked by beta 1,4 glycosidic bonds Cellulose is a linear unbranched chain, each consisting of a single chain. A single type of monomer unit is used to make cellulose. Cellulose is a structural polysaccharide in cell walls of plants.

Keratin
Keratin is a fibrous protein and is important in the making up of the outer layer of human skin. It is also a component of hair and nails. Keratin monomers form bundles that form filaments which are tough and insoluble. They also from tissues found in reptiles, birds, amphibians and mammals. Chitin is the only other biological matter that is as tough as tissues made of keratin.

The structure of keratin.

Keratin is formed by basic macromolecules, polypeptide chains. These chains curl into alpha helices with hydrophobic amino acids. Mammals have about 30 different alpha keratin. The polypeptide chains of keratin are held together by hydrogen bonds. Two alpha helices are coiled together to form a coiled coil

structure, then coiled coils form a Protofilament (crosslinks). Helices of about 300 amino acids with hydrophobic amino acids at every 4th and 7th making a Lucien zipper. Many pairs of coiled coils twist together to form a Photo fibril (4 helices). The coiled formations are packed at higher levels by disulphide bridges and secondary attractive forces. S-S bonds between the polypeptide chains of multihelical chain rope add strength. Of all the amino acids in keratin, cysteine may account for as much as 24%. The numerous disulphide bonds formed by cysteine are responsible for the stability of keratin; it is completely insoluble in water and is not attacked by enzymes that split protein molecules. These enzymes are known as proteolytic enzymes. The length of keratin fibres depends on their water content; complete hydration increase their length by 10% to 20%.

Cysteine- Cysteine transformation.

Hair perming is a basic process that involves the breaking of existing disulphide bonds between alpha helices. The disulphide bonds are broken by applying a reducing agent to the hair, then the hair is arranged into the desired shape and an oxidising agent is applied to reform disulphide bonds.