Bioconformational modulation of a thymidine kinase enzyme ligand through F⋯HO intramolecular hydrogen bond

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorMartins, Francisco A.-
Autor(es): dc.creatorFreitas, Matheus Puggina de-
Data de aceite: dc.date.accessioned2026-02-09T11:22:32Z-
Data de disponibilização: dc.date.available2026-02-09T11:22:32Z-
Data de envio: dc.date.issued2020-09-15-
Data de envio: dc.date.issued2020-09-15-
Data de envio: dc.date.issued2020-06-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/43085-
Fonte completa do material: dc.identifierhttps://doi.org/10.1016/j.jmgm.2020.107545-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1139547-
Descrição: dc.descriptionWhile the induced-fit of a ligand towards an enzyme is pivotally dictated by intermolecular hydrogen bonds between the small molecule and amino acid residues in the binding site, the role of intramolecular hydrogen bond as contributing interaction for a bioactive conformation is not well understood. This work reports a theoretical conformational analysis of a thymidine kinase enzyme ligand (NMF) that is prone to experience an F⋯HO intramolecular hydrogen bond, inside and outside the biological binding site. This interaction stabilizes the most favorable conformations of NMF in the gas phase and, although it can be disrupted in a biological environment due to intermolecular hydrogen bonds in some cases, these interactions are competitive in other systems. Therefore, an intramolecular hydrogen bond can affect the conformational likeliness most related to the bioactivity. Moreover, isolated conformations governed by this interaction cannot be unequivocally used to generate molecular descriptors in 3D-QSAR (Quantitative Structure-Activity Relationships), since the bioactive conformation may not be determined only by intramolecular interactions.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceJournal of Molecular Graphics and Modelling-
Palavras-chave: dc.subjectIntermolecular hydrogen bonds-
Palavras-chave: dc.subjectBioactive conformation-
Palavras-chave: dc.subjectIntramolecular interactions-
Palavras-chave: dc.subjectEnzimas-
Palavras-chave: dc.subjectLigações de hidrogênio intermoleculares-
Palavras-chave: dc.subjectConformação bioativa-
Palavras-chave: dc.subjectInterações intramoleculares-
Título: dc.titleBioconformational modulation of a thymidine kinase enzyme ligand through F⋯HO intramolecular hydrogen bond-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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