Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr (a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged. (b) How many complete turns are there in this helix? (b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why? (c) Which side chains are likely to face the interior of the protein? Why?
1. Consider the following α helix from myoglobin at pH 7.
Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr
(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.
(b) How many complete turns are there in this helix?
(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?
(c) Which side chains are likely to face the interior of the protein? Why?
Proteins are folded polypeptides. Polypeptides are amino acid polymers linked to each other via a peptide bond. As many as 20 different amino acids can be found in all proteins.
Amino acids have a carboxyl group, an amino group and a side group linked to the same carbon called the alpha carbon. Amino acid differ from each other based on the chemical properties of their side group.
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