A conformational preference parameter to predict helices in integral membrane proteins.

J K Mohana Rao; P Argos

doi:10.1016/0167-4838(86)90295-5

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A conformational preference parameter to predict helices in integral membrane proteins.

J K Mohana Rao·P Argos

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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

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Adenosine Triphosphatases Amino Acid Sequence Animals Bacteriorhodopsins Halobacterium Humans Membrane Proteins Protein Conformation Protein Sorting Signals Receptors, Nicotinic Solubility Structure-Activity Relationship Comparative Study Journal Article

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J K Mohana Rao, P Argos. 1986-01-30. A conformational preference parameter to predict helices in integral membrane proteins.. https://doi.org/10.1016/0167-4838(86)90295-5

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