Maiah Beatrice R.

Dinglasan

2EPH

HEMOGLOBIN
Amino Acid Sequence

Secondary Structure

Motif - Each subunit contains regions with a coiled shape; many of the amino acids that make up the polypeptide
chain interact to form this particular structure, called an alpha helix. In an alpha helix, each amino acid is "hydrogenbonded" to the amino acid that is four residues ahead of it in the chain. In hemoglobin, the hydrogen-bonding interaction
occurs between the H of an -NH group and the O of a -CO group of the polypeptide backbone chain; the amino-acid side
chains extend outward from the backbone of the helix. Approximately 75% of the amino-acid composition of hemoglobin
adopts an alpha-helical structure. Another common structural motif is the beta-pleated sheet, in which amino acids line up
in straight parallel rows.
Quaternary Structure

Function The main function of hemoglobin is to transport oxygen from the lungs to the tissues and then
transport CO2 back from the tissues to the lungs.
MYOGLOBIN
Amino Acid Sequence (Horse Heart Myoglobin)

Secondary Structure

Motif motif 1 largely includes helix A; motif 2 spans most of helix B and helix C; motif 3 corresponds to helix E,
and includes the conserved distal His residue; motif 4 corresponds to helix F, and includes the invariant proximal
His residue; motif 5 spans helix G; and motif 6 spans helix H. Motifs 3-5 are adjacent Two iterations on OWL28.2
were required to reach convergence, at which point a true set comprising 79 sequences was identified.
Tertiary Structure

Function Myoglobin contains a heme (prosthetic) group which is responsible for its main function (carrying of
oxygen molecules to muscle tissues). Myoglobin can exist in the oxygen free form, deoxymyoglobin, or in a form
in which the oxygen molecule is bound, called oxymyoglobin.
ELASTIN
Amino Acid Sequence

Secondary Structure

Motif The elastin-like polypeptides are a well-defined family of polymers with noteworthy characteristic based
on the VPGVG repeated motif of bovine elastin.
Function Elastin is a highly elastic protein in connective tissue and allows many tissues in the body to resume
their shape after stretching or contracting.
COLLAGEN
Amino Acid Sequence

Secondary and Quaternary Structure

Motif Fibril associated collagens dont cross link to form fibrils, instead the Gly-X-Y amino acid motif is
regularly interrupted to give non- helical motifs which reult in kinks in the collagen molecule. Additionally, some
propeptides are not removed and so the globular regions will prevent association of the collagens into fibrils.
Instead they mediate interactions between collagen fibrils and other extracellular molecules.
Function Collagen gives the skin its strength and structure, and also plays a role in the replacement of dead
skin cells.

IMMUNOGLOBULIN
Amino Acid Sequence

Secondary Structure

Motif

Quaternary Structure

Function Immunoglobulins are glycoproteins that function as antibodies.

INSULIN
Amino Acid Sequence

Secondary Structure

Motif The interleukin (IL)-4 receptor alpha-chain (IL-4Ralpha) contains a sequence motif
(488PLVIAGNPAYRSFSD) termed the insulin IL-4 receptor motif (I4R motif). Mutation of the central Tyr497 to Phe blocks
the tyrosine phosphorylation of the insulin receptor substrate 1 (IRS1) and diminishes proliferation in response to IL-4.
Tertiary Structure

Quaternary Structure

Function Insulin regulates how the body uses and stores glucose and fat. Many of the body's cells rely on
insulin to take glucose from the blood for energy.
GLUCAGON
Amino Acid Sequence

Secondary Structure

Quaternary Structure

Motif Several uncharacterized proteins interact with the flanking motif (TCATT) of the glucagon CRE
Function The pancreas releases glucagon when the concentration of glucose in the bloodstream falls too low.
Glucagon causes the liver to convert stored glycogen into glucose, which is released into the bloodstream. High
blood-glucose levels stimulate the release of insulin.