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General Theory of Specific Binding: Insights from a Genetic-Mechano-Chemical Protein Model

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dc.contributor.authorJohn M. McBride-
dc.contributor.authorEckmann, Jean-Pierre-
dc.contributor.authorTsvi Tlusty-
dc.date.accessioned2023-01-26T02:32:14Z-
dc.date.available2023-01-26T02:32:14Z-
dc.date.created2022-11-29-
dc.date.issued2022-11-
dc.identifier.issn0737-4038-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/12575-
dc.description.abstractProteins need to selectively interact with specific targets among a multitude of similar molecules in the cell. However, despite a firm physical understanding of binding interactions, we lack a general theory of how proteins evolve high specificity. Here, we present such a model that combines chemistry, mechanics, and genetics and explains how their interplay governs the evolution of specific protein-ligand interactions. The model shows that there are many routes to achieving molecular discrimination-by varying degrees of flexibility and shape/chemistry complementarity-but the key ingredient is precision. Harder discrimination tasks require more collective and precise coaction of structure, forces, and movements. Proteins can achieve this through correlated mutations extending far from a binding site, which fine-tune the localized interaction with the ligand. Thus, the solution of more complicated tasks is enabled by increasing the protein size, and proteins become more evolvable and robust when they are larger than the bare minimum required for discrimination. The model makes testable, specific predictions about the role of flexibility and shape mismatch in discrimination, and how evolution can independently tune affinity and specificity. Thus, the proposed theory of specific binding addresses the natural question of "why are proteins so big?". A possible answer is that molecular discrimination is often a hard task best performed by adding more layers to the protein.-
dc.language영어-
dc.publisherOXFORD UNIV PRESS-
dc.titleGeneral Theory of Specific Binding: Insights from a Genetic-Mechano-Chemical Protein Model-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000879850000001-
dc.identifier.scopusid2-s2.0-85141892429-
dc.identifier.rimsid79292-
dc.contributor.affiliatedAuthorJohn M. McBride-
dc.contributor.affiliatedAuthorTsvi Tlusty-
dc.identifier.doi10.1093/molbev/msac217-
dc.identifier.bibliographicCitationMOLECULAR BIOLOGY AND EVOLUTION, v.39, no.11-
dc.relation.isPartOfMOLECULAR BIOLOGY AND EVOLUTION-
dc.citation.titleMOLECULAR BIOLOGY AND EVOLUTION-
dc.citation.volume39-
dc.citation.number11-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaEvolutionary Biology-
dc.relation.journalResearchAreaGenetics & Heredity-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryEvolutionary Biology-
dc.relation.journalWebOfScienceCategoryGenetics & Heredity-
dc.subject.keywordPlusMOLECULAR-DYNAMICS SIMULATIONS-
dc.subject.keywordPlusENTHALPY-ENTROPY COMPENSATION-
dc.subject.keywordPlusELASTIC NETWORK MODELS-
dc.subject.keywordPlusLIGAND-BINDING-
dc.subject.keywordPlusCONFORMATIONAL ENTROPY-
dc.subject.keywordPlusSHAPE COMPLEMENTARITY-
dc.subject.keywordPlusRECOGNITION-
dc.subject.keywordPlusAFFINITY-
dc.subject.keywordPlusPREDICTION-
dc.subject.keywordPlusEVOLUTION-
dc.subject.keywordAuthormolecular recognition-
dc.subject.keywordAuthorbinding specificity-
dc.subject.keywordAuthorconformational changes-
dc.subject.keywordAuthorprotein evolution-
dc.subject.keywordAuthortRNA synthetase-
Appears in Collections:
Center for Soft and Living Matter(첨단연성물질 연구단) > 1. Journal Papers (저널논문)
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