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dc.creatorBohorquez, Hugo J. 
dc.creatorSuarez, Carlos F. 
dc.creatorPatarroyo, Manuel E. 
dc.date.accessioned2020-08-06T16:20:27Z
dc.date.available2020-08-06T16:20:27Z
dc.date.created2018
dc.identifier.issnISSN: 2045-2322
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/26012
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 (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.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.relation.ispartofScientific reports, ISSN:2045-2322, Vol.8 (2018); pp.7717-
dc.relation.urihttps://www.nature.com/articles/s41598-017-08041-7.pdf
dc.sourceSCIENTIFIC REPORTS
dc.subjectCiencia y tecnología - Otros temas
dc.titleMass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements (vol 7, 7717, 2017)
dc.typearticle
dc.publisherNature Publishing Group
dc.subject.keywordScience & Technology - Other Topics
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.type.spaArtículo
dc.rights.accesoAbierto (Texto Completo)
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.identifier.doihttps://doi.org/10.1038/s41598-018-21981-y
dc.title.TranslatedTitleLa propensión a la masa y estructura secundaria de los aminoácidos explica su mutabilidad y reemplazos evolutivos (vol 7, 7717, 2017)
dc.relation.citationEndPage
dc.relation.citationStartPage7717
dc.relation.citationTitleSCIENTIFIC REPORTS
dc.relation.citationVolumeVol. 8


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