Protein solvation in allosteric regulation: A water effect on hemoglobin

dc.contributor.authorColombo, Marcio F. [UNESP]
dc.contributor.authorRau, Donald C.
dc.contributor.authorParsegian, V. Adrian
dc.contributor.institutionNational Institutes of Health
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2022-04-28T19:53:52Z
dc.date.available2022-04-28T19:53:52Z
dc.date.issued1992-01-01
dc.description.abstractThe 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.en
dc.description.affiliationLaboratory of Biochemistry and Metabolism National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892
dc.description.affiliationPhysical Sciences Laboratory National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892
dc.description.affiliationDepartamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo
dc.description.affiliationUnespDepartamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo
dc.format.extent655-659
dc.identifierhttp://dx.doi.org/10.1126/science.1585178
dc.identifier.citationScience, v. 256, n. 5057, p. 655-659, 1992.
dc.identifier.doi10.1126/science.1585178
dc.identifier.issn0036-8075
dc.identifier.scopus2-s2.0-0026535070
dc.identifier.urihttp://hdl.handle.net/11449/223934
dc.language.isoeng
dc.relation.ispartofScience
dc.sourceScopus
dc.titleProtein solvation in allosteric regulation: A water effect on hemoglobinen
dc.typeArtigo
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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