A conformational preference parameter to predict helices in integral membrane proteins

Biochim Biophys Acta. 1986 Jan 30;869(2):197-214. doi: 10.1016/0167-4838(86)90295-5.

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

Publication types

  • Comparative Study

MeSH terms

  • Adenosine Triphosphatases
  • Amino Acid Sequence
  • Animals
  • Bacteriorhodopsins
  • Halobacterium / ultrastructure
  • Humans
  • Membrane Proteins*
  • Protein Conformation
  • Protein Sorting Signals
  • Receptors, Nicotinic
  • Solubility
  • Structure-Activity Relationship

Substances

  • Membrane Proteins
  • Protein Sorting Signals
  • Receptors, Nicotinic
  • Bacteriorhodopsins
  • Adenosine Triphosphatases