How to describe the structure of insulin, keratin, fibroin, myoglobin and haemoglobin?
Answers
Answer:
Keratin makes up hair and nails.
Insulin is a protein produced by the pancreas and which circulates in the blood and regulates blood sugar levels.
Myoglobin is an oxygen-storage protein found in the muscle cells.
The hemoglobin molecule contains four separate folded peptide chains, which form a hydrophobic or water 'repelling' pocket around a heme group. The heme group is composed of a central iron atom complexed to four nitrogen atoms.
Explanation:
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Answer:
Insulin is composed of two peptide chains referred to as the A chain and B chain. A and B chains are linked together by two disulfide bonds, and an additional disulfide is formed within the A chain. In most species, the A chain consists of 21 amino acids and the B chain of 30 amino acids.
α-keratin is a fibrous structural protein, meaning it is made up of amino acids that form a repeating secondary structure. ... The secondary structure of α-keratin is very similar to that of a traditional protein α-helix and forms a coiled coil.
Keratin is rich in the amino acid cysteine, and it has the ability to self-assemble into bundles of fibers. Within these fiber bundles, individual strands are further crosslinked through S-S (sulfur-sulfur) bonds involving the cysteine side chains.
fibroin protein consists of layers of antiparallel beta sheets. Its primary structure mainly consists of the recurrent amino acid sequence (Gly-Ser-Gly-Ala-Gly-Ala)n. ... Fibroin is known to arrange itself in three structures, called silk I, II, and III.
Myoglobin is a single-chain globular protein with the heme prosthetic group in the center. The Iron located at the center of heme group interacts with six ligands, the four nitrogen atoms of the porphyrin ring, an imidazole side chain of amino acid residue His-64, and an oxygen molecule
hemoglobin molecule contains four separate folded peptide chains, which form a hydrophobic or water 'repelling' pocket around a heme group. The heme group is composed of a central iron atom complexed to four nitrogen atoms. Oxygen is capable of reversibly binding to the heme unit in a process known as oxygenation.