Protein Surface Interactions—Theoretical and Experimental Studies

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorFederal University of Rio de Janeiro-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorAlmeida, Fabio C. L.-
Autor(es): dc.creatorSanches, Karoline [UNESP]-
Autor(es): dc.creatorPinheiro-Aguiar, Ramon-
Autor(es): dc.creatorAlmeida, Vitor S.-
Autor(es): dc.creatorCaruso, Icaro P. [UNESP]-
Data de aceite: dc.date.accessioned2022-08-04T22:10:37Z-
Data de disponibilização: dc.date.available2022-08-04T22:10:37Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2021-07-09-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.3389/fmolb.2021.706002-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/222030-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/222030-
Descrição: dc.descriptionIn this review, we briefly describe a theoretical discussion of protein folding, presenting the relative contribution of the hydrophobic effect versus the stabilization of proteins via direct surface forces that sometimes may be overlooked. We present NMR-based studies showing the stability of proteins lacking a hydrophobic core which in turn present hydrophobic surface clusters, such as plant defensins. Protein dynamics measurements by NMR are the key feature to understand these dynamic surface clusters. We contextualize the measurement of protein dynamics by nuclear relaxation and the information available at protein surfaces and water cavities. We also discuss the presence of hydrophobic surface clusters in multidomain proteins and their participation in transient interactions which may regulate the function of these proteins. In the end, we discuss how surface interaction regulates the reactivity of certain protein post-translational modifications, such as S-nitrosation.-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionInstitute of Medical Biochemistry—IBqM Federal University of Rio de Janeiro-
Descrição: dc.descriptionNational Center for Structural Biology and Bioimaging (CENABIO) National Center for Nuclear Magnetic Resonance (CNRMN) Federal University of Rio de Janeiro-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP)-
Descrição: dc.descriptionMultiuser Center for Biomolecular Innovation (CMIB) Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University “Júlio de Mesquita Filho” (UNESP)-
Descrição: dc.descriptionFAPERJ: 255.940/2020 202.279/2018 239.229/2018 210.361/2015 204.432/2014-
Descrição: dc.descriptionCNPq: 309564/2017-4-
Idioma: dc.languageen-
Relação: dc.relationFrontiers in Molecular Biosciences-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectclusters-
Palavras-chave: dc.subjectdynamics-
Palavras-chave: dc.subjecthydrophobic surface clusters-
Palavras-chave: dc.subjectinterdomain-
Palavras-chave: dc.subjectNMR-
Palavras-chave: dc.subjectsolvation-
Palavras-chave: dc.subjectsurface-
Título: dc.titleProtein Surface Interactions—Theoretical and Experimental Studies-
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