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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
2
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|
pubmed:dateCreated |
1986-3-17
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pubmed:abstractText |
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 discussed
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pubmed:language |
eng
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pubmed:journal |
|
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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|
pubmed:issn |
0006-3002
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
30
|
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pubmed:volume |
869
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
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pubmed:pagination |
197-214
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pubmed:dateRevised |
2006-11-15
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|
pubmed:meshHeading |
pubmed-meshheading:2935194-Adenosine Triphosphatases,
pubmed-meshheading:2935194-Amino Acid Sequence,
pubmed-meshheading:2935194-Animals,
pubmed-meshheading:2935194-Bacteriorhodopsins,
pubmed-meshheading:2935194-Halobacterium,
pubmed-meshheading:2935194-Humans,
pubmed-meshheading:2935194-Membrane Proteins,
pubmed-meshheading:2935194-Protein Conformation,
pubmed-meshheading:2935194-Protein Sorting Signals,
pubmed-meshheading:2935194-Receptors, Nicotinic,
pubmed-meshheading:2935194-Solubility,
pubmed-meshheading:2935194-Structure-Activity Relationship
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pubmed:year |
1986
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pubmed:articleTitle |
A conformational preference parameter to predict helices in integral membrane proteins.
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pubmed:publicationType |
Journal Article,
Comparative Study
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