Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements: Publisher Correction: Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements (Scientific reports (2017) 7 1 (7717))

Hugo J. Bohórquez, Carlos F. Suárez, Manuel E. Patarroyo

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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, Phe 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 (\overline{R} R = 0.85) between thirty amino acid mutability scales and the mutational inertia (I X ), which measures the energetic cost weighted by the number of observations at the most probable amino acid conformation. These results indicate that amino acid substitutions follow two optimally-efficient principles: (a) amino acids interchangeability privileges their secondary structural similarity, and (b) the amino acid mutability depends directly on its biosynthetic energy cost, and inversely with its frequency. These two principles are the underlying rules governing the observed amino acid substitutions.

Original languageEnglish (US)
Article number7717
Number of pages1
JournalScientific Reports
Volume7
Issue number1
DOIs
StatePublished - Dec 1 2017

All Science Journal Classification (ASJC) codes

  • General

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