The subdomain structure of human serum albumin in solution under different pH conditions studied by small angle X-ray scattering

dc.contributorLAB NACL LUZ SINCROTRON
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorOlivieri, J. R. [UNESP]
dc.creatorCraievich, A. F. [UNESP]
dc.date2014-05-27T11:17:58Z
dc.date2014-05-27T11:17:58Z
dc.date1995-01-01
dc.date.accessioned2023-09-12T07:50:41Z
dc.date.available2023-09-12T07:50:41Z
dc.identifierhttp://dx.doi.org/10.1007/BF00211402
dc.identifierEuropean Biophysics Journal, v. 24, n. 2, p. 77-84, 1995.
dc.identifier0175-7571
dc.identifierhttp://hdl.handle.net/11449/132352
dc.identifier10.1007/BF00211402
dc.identifierWOS:A1995TE48200004
dc.identifier2-s2.0-0028837623
dc.identifier2406867656111498
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8781631
dc.descriptionSmall-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.
dc.descriptionLAB NACL LUZ SINCROTRON,SAO PAULO,BRAZIL
dc.descriptionUNIV SAO PAULO,INST FIS,BR-05508 SAO PAULO,BRAZIL
dc.descriptionDepartamento de Fisica UNESP, CP 136, Sao Jose do Rio Preto-SP, CEP 15054
dc.format77-84
dc.languageeng
dc.publisherSpringer
dc.relationEuropean Biophysics Journal
dc.relation1.935
dc.relation0,604
dc.rightsAcesso restrito
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 scattering
dc.typeArtigo


Este ítem pertenece a la siguiente institución