Você está no menu de acessibilidade

Utilize este identificador para citar ou criar um link para este item: http://acervodigital.unesp.br/handle/11449/132352
Registro de metadados completo
Campo DCValorIdioma
dc.contributor.authorOlivieri, J. R.-
dc.contributor.authorCraievich, A. F.-
dc.date.accessioned2014-05-27T11:17:58Z-
dc.date.accessioned2016-10-25T21:25:38Z-
dc.date.available2014-05-27T11:17:58Z-
dc.date.available2016-10-25T21:25:38Z-
dc.date.issued1995-01-01-
dc.identifierhttp://dx.doi.org/10.1007/BF00211402-
dc.identifier.citationEuropean Biophysics Journal, v. 24, n. 2, p. 77-84, 1995.-
dc.identifier.issn0175-7571-
dc.identifier.urihttp://hdl.handle.net/11449/132352-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/132352-
dc.description.abstractSmall-angle X-ray scattering (SAXS) was used to study structural characteristics of human serum albumin (HSA) in solution under different pH conditions. Guinier analysis of SAXS results yielded values of the molecular radius of gyration ranging from 26.7 Å to 34.5 Å for pH varying from 2.5 to 7.0. This suggests the existence of significant differences in the overall shape of the molecule at different pH. Molecular models based on subdomains with different spatial configurations were proposed. The distance distribution functions associated with these models were calculated and compared with those determined from the experimental SAXS intensity functions. The conclusion of this SAXS study is that the arrangement of molecular subdomains is clearly pH dependent; the molecule adopting more or less compact configuration for different pH conditions. The conclusions of this systematic study on the modification in molecular shape of HSA as a response to pH changes is consistent with those of previous investigations performed for particular pH conditions.en
dc.format.extent77-84-
dc.language.isoeng-
dc.publisherSpringer-
dc.sourceScopus-
dc.subjectHuman serum albumin-
dc.subjectMolacular configuration-
dc.subjectSAXS-
dc.subjectAlbumin-
dc.subjectPh-
dc.subjectProtein structure-
dc.subjectRadiation scattering-
dc.subjectChemistry, Physical-
dc.subjectHuman-
dc.subjectHydrogen-Ion Concentration-
dc.subjectProtein Conformation-
dc.subjectScattering, Radiation-
dc.subjectSerum Albumin-
dc.subjectSolutions-
dc.subjectSupport, Non-U.S. Gov't-
dc.subjectX-Rays-
dc.titleThe subdomain structure of human serum albumin in solution under different pH conditions studied by small angle X-ray scatteringen
dc.typeoutro-
dc.contributor.institutionLAB NACL LUZ SINCROTRON-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationLAB NACL LUZ SINCROTRON,SAO PAULO,BRAZIL-
dc.description.affiliationUNIV SAO PAULO,INST FIS,BR-05508 SAO PAULO,BRAZIL-
dc.description.affiliationUnespDepartamento de Fisica UNESP, CP 136, Sao Jose do Rio Preto-SP, CEP 15054-
dc.identifier.doi10.1007/BF00211402-
dc.identifier.wosWOS:A1995TE48200004-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofEuropean Biophysics Journal-
dc.identifier.scopus2-s2.0-0028837623-
Aparece nas coleções:Artigos, TCCs, Teses e Dissertações da Unesp

Não há nenhum arquivo associado com este item.
 

Itens do Acervo digital da UNESP são protegidos por direitos autorais reservados a menos que seja expresso o contrário.