title: A conformational preference parameter to predict helices in integral membrane proteins.
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 discussed
mesh_terms: D000251:Adenosine Triphosphatases; D000595:Amino Acid Sequence; D000818:Animals; D001436:Bacteriorhodopsins; D006217:Halobacterium / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins; D011487:Protein Conformation; D021382:Protein Sorting Signals; D011978:Receptors, Nicotinic; D012995:Solubility; D013329:Structure-Activity Relationship
chemical_list: D008565:Membrane Proteins; D021382:Protein Sorting Signals; D011978:Receptors, Nicotinic; D001436:Bacteriorhodopsins; D000251:Adenosine Triphosphatases