Protein solvation in allosteric regulation: A water effect on hemoglobin

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorNational Institutes of Health-
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorColombo, Marcio F.-
Autor(es): dc.creatorRau, Donald C.-
Autor(es): dc.creatorParsegian, V. Adrian-
Data de aceite: dc.date.accessioned2025-08-21T22:35:29Z-
Data de disponibilização: dc.date.available2025-08-21T22:35:29Z-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued2022-04-28-
Data de envio: dc.date.issued1992-01-01-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1126/science.1585178-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/223934-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/223934-
Descrição: dc.descriptionThe oxygen affinity of hemoglobin varies linearly with the chemical potential of water in the bathing medium, as seen from the osmotic effect of several neutral solutes, namely sucrose, stachyose, and two polyethyleneglycols (molecular weights of 150 and 400). The data, analyzed either by Wyman linkage equations or by Gibbs-Duhem relations, show that -60 extra water molecules bind to hemoglobin during the transition from the fully deoxygenated tense (T) state to the fully oxygenated relaxed (R) state. This number, independent of the nature of the solute, agrees with the difference in water-accessible surface areas previously computed for the two conformations. The work of solvation in allosteric regulation can no longer go unrecognized.-
Descrição: dc.descriptionLaboratory of Biochemistry and Metabolism National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892-
Descrição: dc.descriptionPhysical Sciences Laboratory National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892-
Descrição: dc.descriptionDepartamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo-
Descrição: dc.descriptionDepartamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo-
Formato: dc.format655-659-
Idioma: dc.languageen-
Relação: dc.relationScience-
???dc.source???: dc.sourceScopus-
Título: dc.titleProtein solvation in allosteric regulation: A water effect on hemoglobin-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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