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

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dc.creatorBohórquez, Hugo J.spa
dc.creatorSuárez, Carlos F.spa
dc.creatorPatarroyo, Manuel E.spa
dc.date.accessioned2020-05-26T00:00:54Z
dc.date.available2020-05-26T00:00:54Z
dc.date.created2017spa
dc.description.abstractWhy 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. © 2017 The Author(s).eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1038/s41598-017-08041-7
dc.identifier.issn20452322
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/23284
dc.language.isoengspa
dc.publisherNature Publishing Groupspa
dc.relation.citationIssueNo. 1
dc.relation.citationTitleScientific Reports
dc.relation.citationVolumeVol. 7
dc.relation.ispartofScientific Reports, ISSN:20452322, Vol.7, No.1 (2017)spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85042941481&doi=10.1038%2fs41598-017-08041-7&partnerID=40&md5=6d6943620354c2adb0dd5b2f6f79f913spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordaminoacidsspa
dc.subject.keywordmutabilityspa
dc.subject.keywordevolutionaryspa
dc.subject.keywordreplacementsspa
dc.titleMass and secondary structure propensity of amino acids explain their mutability and evolutionary replacementsspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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