A conformational preference parameter to predict helices in integral membrane proteins

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

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Volume 869, Issue 2, 30 January 1986, Pages 197-214

Biochimica et Biophy...

https://doi.org/10.1016/0167-4838(86)90295-5 Get rights and content

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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A conformational preference parameter to predict helices in integral membrane proteins

Abstract

Trends Biochem. Sci.

J. Mol. Biol.

Trends Biochem. Sci.

J. Theor. Biol.

FEBS Lett.

Biochim. Biophys. Acta

Cell

J. Mol. Biol.

Cell

J. Biol. Chem.

J. Biol. Chem.

Cell

J. Biol. Chem.

FEBS Lett.

J. Mol. Biol.

Trends Biochem. Sci.

J. Biol. Chem.

Progr. Retin. Res.

J. Mol. Biol.

FEBS Lett.

FEBS Lett.

FEBS Lett.

Cell

Membrane Biol.

Sci. Am.

J. Cell. Biol.

J. Bioenerg. Biomembranes

Annu. Rev. Biochem.

Nature (London)

Biochemistry

Biochemistry

Science

Eur. J. Biochem.

Biophys. J.

Biochemistry

Eur. J. Biochem.

Biophys. Struct. Mech.

Nature (London)