Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements.

ABSTRACT: Why is an amino acid replacement in a protein accepted during evolution? The answer given by bioinformatics relies on the frequency of change of each amino acid by another one and the propensity of each to remain unchanged. We propose that these replacement rules are recoverable from the secondary structural trends of amino acids. A distance measure between high-resolution Ramachandran distributions reveals that structurally similar residues coincide with those found in substitution matrices such as BLOSUM: Asn ↔ Asp, P™he ↔ Tyr, Lys ↔ Arg, Gln ↔ Glu, Ile ↔ Val, Met → Leu; with Ala, Cys, His, Gly, Ser, Pro, and Thr, as structurally idiosyncratic residues. We also found a high average correlation ([Formula: see text] = 0.85) between thirty amino acid mutability scales and the mutational ine

SUBMITTER: Bohorquez HJ 

PROVIDER: S-EPMC5552740 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature