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dc.contributor.authorBohórquez, Hugo J.spa
dc.contributor.authorSuárez, Carlos F.spa
dc.contributor.authorPatarroyo, Manuel Elkinspa
dc.date.accessioned2019-09-19T19:14:40Zspa
dc.date.available2019-09-19T19:14:40Zspa
dc.date.issued2017spa
dc.identifier.citationBohórquez, H.J., Suárez, C.F., Patarroyo, M.E. Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements (2017) Scientific Reports, 7 (1), art. no. 7717,spa
dc.identifier.issn2045-2322spa
dc.identifier.urihttps://www.nature.com/articles/s41598-017-08041-7spa
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/pdfspa
dc.language.isoengspa
dc.relation.ispartofseriesScientific Reports;Vol., 7, No.1 Dic. 1, 2017 páginas 1-12spa
dc.rightsDerechos Reservados - Universidad de Ciencias Aplicadas y Ambientalesspa
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/4.0/spa
dc.sourcehttps://www.nature.com/articles/s41598-017-08041-7spa
dc.sourcehttps://udca.elogim.com:2092/record/display.uri?eid=2-s2.0-85042941481&origin=resultslist&sort=plf-f&src=s&nlo=&nlr=&nls=&sid=a80a3576a0a2fb49af70980cb85af4ec&sot=a&sdt=sisr&sl=23&s=SOURCE-ID+%2821100200805%29&ref=%28Mass+%26+secondary+structure+propensity+of+amino+acids+explain+their+mutability+and+evolutionary+replacements%29&relpos=2&citeCnt=0&searchTerm=spa
dc.subject.meshPéptidosspa
dc.subject.meshProteinasspa
dc.titleMass & secondary structure propensity of amino acids explain their mutability and evolutionary replacementsspa
dc.typeArtículo de revistaspa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.identifier.doi10.1038/s41598-017-08041-7spa
dc.rights.creativecommonsAtribución-NoComercial-CompartirIgual 4.0 Internacional (CC BY-NC-SA 4.0)spa
dc.subject.proposalPeptidesspa
dc.subject.proposalProteinsspa
dc.subject.proposalConformational preferencesspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.driverinfo:eu-repo/semantics/articlespa
dc.type.versioninfo:eu-repo/semantics/publishedVersionspa
dc.subject.agrovocAminoácidosspa
dc.type.contentTextspa
dc.type.redcolhttp://purl.org/redcol/resource_type/ARTspa
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85spa


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