Protein solvation in allosteric regulation: A water effect on hemoglobin
dc.contributor.author | Colombo, Marcio F. [UNESP] | |
dc.contributor.author | Rau, Donald C. | |
dc.contributor.author | Parsegian, V. Adrian | |
dc.contributor.institution | National Institutes of Health | |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | |
dc.date.accessioned | 2022-04-28T19:53:52Z | |
dc.date.available | 2022-04-28T19:53:52Z | |
dc.date.issued | 1992-01-01 | |
dc.description.abstract | The 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.affiliation | Laboratory of Biochemistry and Metabolism National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892 | |
dc.description.affiliation | Physical Sciences Laboratory National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892 | |
dc.description.affiliation | Departamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo | |
dc.description.affiliationUnesp | Departamento de Física IBILCE-UNESP São José do Rio Prêto, São Paulo | |
dc.format.extent | 655-659 | |
dc.identifier | http://dx.doi.org/10.1126/science.1585178 | |
dc.identifier.citation | Science, v. 256, n. 5057, p. 655-659, 1992. | |
dc.identifier.doi | 10.1126/science.1585178 | |
dc.identifier.issn | 0036-8075 | |
dc.identifier.scopus | 2-s2.0-0026535070 | |
dc.identifier.uri | http://hdl.handle.net/11449/223934 | |
dc.language.iso | eng | |
dc.relation.ispartof | Science | |
dc.source | Scopus | |
dc.title | Protein solvation in allosteric regulation: A water effect on hemoglobin | en |
dc.type | Artigo | |
unesp.campus | Universidade Estadual Paulista (Unesp), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Preto | pt |
unesp.department | Física - IBILCE | pt |