Structural function of antibodies?!Watch
Good evening, i have had great help(piggy) from this website in the past and hopefully this will not be the exception. I am currently stuck trying to find out how the structure of collagen helps fulfil its function. If there is anyone out there that could shed some light on this i would greatly appreciate it. You will have my eternal thanks. Without sticking the hand in, i could use help with antibodies swell if there is any help going. Thank you
Globular - These tend to form ball-like structures where hydrophobic parts are towards the centre and hydrophilic are towards the edges, which makes them water soluble. They usually have metabolic roles, for example: enzymes in all organisms, plasma proteins and antibodies in mammals.
Fibrous - They proteins form long fibres and mostly consist of repeated sequences of amino acids which are insoluble in water. They usually have structural roles, such as: Collagen in bone and cartilage, Keratin in fingernails and hair.
Collagen is a fibrous protein consisting of three polypeptide chains wound around each other. Each of the three chains is a coil itself. Hydrogen bonds form between these coils, which are around 1000 amino acids in length, which gives the structure strength. This is important given collagen's role, as structural protein. This strength is increased by the fact that collagen molecules form further chains with other collagen molecules and form Covalent Cross Links with each other, which are staggered along the molecules to further increase stability. Collagen molecules wrapped around each other form Collagen Fibrils which themselves form Collagen Fibres.
Collagen has many functions:
1) Form the structure of bones
2) Makes up cartilage and connective tissue
3) Prevents blood that is being pumped at high pressure from bursting the walls of arteries
4) Is the main component of tendons, which connect skeletal muscles to bones
NB: Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. The amino acid sequence in the tips of the "Y" varies greatly among different antibodies. This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen. The variable region includes the ends of the light and heavy chains. Treating the antibody with a protease can cleave this region, producing Fab or fragment antigen binding that include the variable ends of an antibody. Material used for the studies shown below originated from Fab.
The constant region determines the mechanism used to destroy antigen. Antibodies are divided into five major classes, IgM, IgG, Iga, IgD, and IgE, based on their constant region structure and immune function.