What is the significance of the hydrophobic side chain each 3rd or 4th residue in an alpha-keratin?
Amino acids form a linear chain to give shape to the primary
structure of a protein. This primary structure of a protein then
folds into the secondary structure, -helix and
-sheet. The
folding of the primary structure into a secondary structure takes
place due to non-covalent and hydrophobic interactions between the
amino acid side chains and the amino acid side chain and the
environment.
-keratin is rich
in alanine, leucine, arginine, and cysteine and has the structure
right-handed
-helix. In such
alpha helices, every N−H group of the backbone donates an H-bond to
the C=O group of the amino acid located 3 or 4 residues earlier
along the protein sequence in the backbone. Hence, the hydrophobic
side chains of each 3rd or 4th residue in an alpha keratin strand
are responsible for the formation of an appropriate secondary alpha
helix structure of the protein.
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What is the significance of the hydrophobic side chain each 3rd or 4th residue in an...
IFor each molecule of FADH_2 that donates electrons to the electron transport chain, ATPs will be produced 1.5 2 2.5 3 10 For questions 9-18, match the description on the left with the correct amino acid on the right. Answers will only be used once. the only achiral amino acid methionine the side chain of this amino acid has an alcohol group glycine an amino acid with an aromatic group glutamate an ammo acid with an acidic side chain tryptophan...
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The pK of the side chain of amino acid X in a polypeptide is normally in the range of 9-10 and carries a positive charge when protonated. Suppose you have a soluble globular protein and you find there is an X that has a pK of 6.5. What is the most likely reason for such a large drop in pK? Circle the correct answer. a) X is on the surface of the protein where it ion pairs with the carboxylate...
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