Linked Life Data

8827450

Source:http://linkedlifedata.com/resource/pubmed/id/8827450

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1996-12-17
pubmed:abstractText
The bacterial opsins can be refolded to regenerate the chromophore by transfer from SDS to DMPC/CHAPS/SDS mixed micelles in the presence of retinal. A sequential refolding model has been proposed for bacterioopsin [Booth et al. (1995) Nature Struct. Biol. 2, 139-143]. However, the roles of DMPC and CHAPS in the refolding process are not clear. In this study we measured the effects of DMPC and CHAPS on the refolding of bacterial opsins in vitro by CD and fluorescence spectroscopy. In contrast to in experiments in the presence of large amounts of DMPC, the process of retinal binding pocket formation was a rate-determining step in overall chromophore regeneration with relatively low concentrations of DMPC. CHAPS triggered alpha-helix formation and long-range interactions between the helices within 1 s by providing a suitable hydrophobic environment for bacterial opsins. This CHAPS-induced transient molten globule-like structure would be identical to I1 postulated by Booth et al., to which DMPC bound and induced the proper packing of the side chains to form a retinal binding pocket. If DMPC was not present, CHAPS induced another conformation change in bacterial opsins, which led to denaturation. DMPC dependence of chromophore regeneration and the maintenance of the retinal binding pocket suggested that retinal binding pocket formation was part of the large structure changes during stable apoprotein formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1143-9
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Dual roles of DMPC and CHAPS in the refolding of bacterial opsins in vitro.
pubmed:affiliation
Department of Biology, School of Science, Nagoya University, Aichi. ysugiya@bio.nagoya-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't