The prediction of the conformation of membrane proteins from the sequence of amino acids.
The methods of Chou & Fasman [Biochemistry (1974) 13, 211-222, 222-245] and of Lim [J. Mol. Biol. (1974)88, 857-872, 873-894] for predicting secondary structure from amino acid sequence have been applied to five predominantly helical membrane-associated peptides. The predictions from the method of Lim (1974a,b) are consistent with the experimental observations, whereas those from Chou & Fasman (1974a,b), although not inconsistent with alpha-helix, favour a beta-structure for several very hydrophobic regions. The results may be rationalized in terms of the effect of the solvent on the conformation of a polypeptide.
19 references, click to expand
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Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins.Biochemistry. 1974 Jan 15;13(2):211-22 PMID: 4358939
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Comparison of predicted and experimentally determined secondary structure of adenyl kinase.Nature. 1974 Jul 12;250(462):140-2 PMID: 4367211
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Red cell membrane glycoprotein: amino acid sequence of an intramembranous region.Biochem Biophys Res Commun. 1972 Nov 15;49(4):964-9 PMID: 4641718
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The amino acid sequence of the B-protein of bacteriophage ZJ-2.Biochem J. 1972 Mar;127(1):167-78 PMID: 5073740
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The conformation of glucagon: predictions and consequences.Biochemistry. 1975 Jun 3;14(11):2536-41 PMID: 1138871
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The beta conformation of polypeptides of valine, isoleucine, and threonine in solution and solid-state: optical and infrared studies.Biopolymers. 1975 Mar;14(3):605-31 PMID: 1174682
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Primary structure and sidechain interactions of PFL filamentous bacterial virus coat protein.Nature. 1975 Jan 3;253(5486):68-71 PMID: 1110754
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Volume and sound velocity changes accompanying the -helix to -form and coil to -helix transitions in aqueous solution.Biopolymers. 1971;10(12):2569-79 PMID: 5126526
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