| Literature DB >> 2935194 |
Abstract
Assignments were made for helical regions in several integral membrane proteins using an algorithm devised to delineate the transmembrane helices in bacteriorhodopsin (Eur. J. Biochem. 182 (1982) 565-575). A new conformational preference parameter for membrane-buried helices was obtained. The use of this parameter to predict helices in membrane proteins is discussed. When applied to the L and M subunits of Rhodopseudomonas sphaeroides, five helices were predicted, which is consistent with the three-dimensional X-ray crystal structure. Data on signal sequences and amino acid exchanges in membrane proteins are also analysed and discussedEntities:
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Year: 1986 PMID: 2935194 DOI: 10.1016/0167-4838(86)90295-5
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002