Crystallization and X-ray diffraction data analysis of human deoxyhaemoglobin A(0) fully stripped of any anions

Página do item simplificado
dc.contributor.authorSeixas, FAV
dc.contributor.authorde Azevedo, W. F.
dc.contributor.authorColombo, M. F.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:30:01Z
dc.date.available2014-05-20T15:30:01Z
dc.date.issued1999-11-01
dc.description.abstractIn this work, initial crystallographic studies of human haemoglobin (Hb) crystallized in isoionic and oxygen-free PEG solution are presented. Under these conditions, functional measurements of the O-2-linked binding of water molecules and release of protons have evidenced that Hb assumes an unforeseen new allosteric conformation. The determination of the high-resolution structure of the crystal of human deoxy-Hb fully stripped of anions may provide a structural explanation for the role of anions in the allosteric properties of Hb and, particularly, for the influence of chloride on the Bohr effect, the mechanism by which Hb oxygen affinity is regulated by pH. X-ray diffraction data were collected to 1.87 Angstrom resolution using a synchrotron-radiation source. Crystals belong to the space group P2(1)2(1)2 and preliminary analysis revealed the presence of one tetramer in the asymmetric unit. The structure is currently being refined using maximum-likelihood protocols.en
dc.description.affiliationUniv Estadual Paulista, Dept Fis, Inst Biociencias Letras & Ciências Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Fis, Inst Biociencias Letras & Ciências Exatas, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.format.extent1914-1916
dc.identifierhttp://dx.doi.org/10.1107/S0907444999009750
dc.identifier.citationActa Crystallographica Section D-biological Crystallography. Copenhagen: Munksgaard Int Publ Ltd, v. 55, p. 1914-1916, 1999.
dc.identifier.doi10.1107/S0907444999009750
dc.identifier.fileWOS000083951500022.pdf
dc.identifier.issn0907-4449
dc.identifier.lattes3425817209646054
dc.identifier.urihttp://hdl.handle.net/11449/39474
dc.identifier.wosWOS:000083951500022
dc.language.isoeng
dc.publisherMunksgaard Int Publ Ltd
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallography
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleCrystallization and X-ray diffraction data analysis of human deoxyhaemoglobin A(0) fully stripped of any anionsen
dc.typeArtigo
dcterms.licensehttp://journals.iucr.org/services/copyrightpolicy.html
dcterms.rightsHolderMunksgaard Int Publ Ltd
unesp.author.lattes3425817209646054
unesp.author.orcid0000-0002-0117-6919[1]
unesp.author.orcid0000-0003-3035-3926[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

Arquivos

Pacote Original
Agora exibindo 1 - 1 de 1
Imagem de Miniatura
Nome:
WOS000083951500022.pdf
Tamanho:
104.87 KB
Formato:
Adobe Portable Document Format
Baixar
Licença do Pacote
Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Artigos - Física - IBILCE