Question

Mayoglobin has 153 amino acid. If it is a complete stretch of alpha helix the length of mayoglobin will be

Answer 1

Answer:

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Explanation:

Myoglobin is a relatively small protein of mass 17.8kDa made up of 153 amino acids in a single polypeptide chain. It was the first protein to have its three-dimensional structure determined by x-ray crystallography by John Kendrew in 1957. Myoglobin is a typical globular protein in that it is a highly folded compact structure with most of the hydrophobic amino acid residues buried in the interior and many of the polar residues on the surface. X-ray crystallography revealed that the single polypeptide chain of myoglobin consist entirely of alpha-helical secondary structure. In fact there are eight alpha-helical secondary structure in myoglobin. Within a hydrophobic cervice formed by the folding of the polypeptide chain is the heme prosthetic group. This nonpolypeptide unit is noncovalently bound to myoglobin and is essential for the biological activity of the protein. Myoglobin is a small oxygen-binding protein found in muscle cells. Its functions primarily in storing oxygen and facilitating oxygen diffusion in muscle tissue. Myoglobin is a single-chain globular protein that consists of 153 amino acids and a heme group (an iron-containing porphyrin). The globular structure of myoglobin consists mainly of alpha helices linked together by various turns. Myoglobin exists either in an oxygen free-form called deoxymyoglobin or in a oxygen bound form called oxymyoglobin. Whether myoglobin binds to oxygen depends on the presence of the prosthetic group, heme. When myoglobin is able to bind to oxygen, it serves as the primary oxygen-carrying molecule in muscle tissue. Normally, the iron group in myoglobin has an oxidation state of 2+. However, when oxygen binds to the iron, it gets oxidized to an oxidation state of 3+. This allows the oxygen that is binded to have a negative charge, which stabilizes it. Myoglobin's affinity for oxygen is higher than hemoglobin. And unlike hemoglobin which is found in the red blood cells, myoglobin is found in muscle tissues.

Answer 2

A N S W E R :

Myoglobin is present in the " Red Muscle Fibers "

E X T R A I N F O R M A T I O N :

Myoglobin is an important haem - containing globular protein.

Myoglobin is an oxygen storing protein.

Myoglobin is abundant especially in the muscles of the diving mammals such as whales, porpoises, dolphins, etc.

Myoglobin is also present in the muscles of diving birds like penguins.

Myoglobin stores oxygen in the form of " Oxymyoglobin ".

Oxymyoglobin releases oxygen.

The oxygen released by Oxymyoglobin is untilised during the process of constraction of muscles.

Myoglobin consists of only one " Haem " group.

Myoglobin can carry only one molecule of Oxygen.

The oxygen dissociation curve of myoglobin is a simple hyperbola.