Protein solvation in allosteric regulation: A water effect on hemoglobin
Autor(a) principal: | |
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Data de Publicação: | 1992 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1126/science.1585178 http://hdl.handle.net/11449/223934 |
Resumo: | 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. |
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Repositório Institucional da UNESP |
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spelling |
Protein solvation in allosteric regulation: A water effect on hemoglobinThe 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.Laboratory of Biochemistry and Metabolism National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892Physical Sciences Laboratory National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892Departamento de Física IBILCE-UNESP São José do Rio Prêto, São PauloDepartamento de Física IBILCE-UNESP São José do Rio Prêto, São PauloNational Institutes of HealthUniversidade Estadual Paulista (UNESP)Colombo, Marcio F. [UNESP]Rau, Donald C.Parsegian, V. Adrian2022-04-28T19:53:52Z2022-04-28T19:53:52Z1992-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article655-659http://dx.doi.org/10.1126/science.1585178Science, v. 256, n. 5057, p. 655-659, 1992.0036-8075http://hdl.handle.net/11449/22393410.1126/science.15851782-s2.0-0026535070Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScienceinfo:eu-repo/semantics/openAccess2022-04-28T19:53:52Zoai:repositorio.unesp.br:11449/223934Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:06:01.520042Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
title |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
spellingShingle |
Protein solvation in allosteric regulation: A water effect on hemoglobin Colombo, Marcio F. [UNESP] |
title_short |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
title_full |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
title_fullStr |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
title_full_unstemmed |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
title_sort |
Protein solvation in allosteric regulation: A water effect on hemoglobin |
author |
Colombo, Marcio F. [UNESP] |
author_facet |
Colombo, Marcio F. [UNESP] Rau, Donald C. Parsegian, V. Adrian |
author_role |
author |
author2 |
Rau, Donald C. Parsegian, V. Adrian |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
National Institutes of Health Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Colombo, Marcio F. [UNESP] Rau, Donald C. Parsegian, V. Adrian |
description |
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. |
publishDate |
1992 |
dc.date.none.fl_str_mv |
1992-01-01 2022-04-28T19:53:52Z 2022-04-28T19:53:52Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1126/science.1585178 Science, v. 256, n. 5057, p. 655-659, 1992. 0036-8075 http://hdl.handle.net/11449/223934 10.1126/science.1585178 2-s2.0-0026535070 |
url |
http://dx.doi.org/10.1126/science.1585178 http://hdl.handle.net/11449/223934 |
identifier_str_mv |
Science, v. 256, n. 5057, p. 655-659, 1992. 0036-8075 10.1126/science.1585178 2-s2.0-0026535070 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Science |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
655-659 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129490230968320 |