Our current level of understanding of membrane-protein folding is primitive, but it is beginning to advance. Previously [Choma, Gratkowski, Lear and DeGrado (2000) Nat. Struct. Biol. 7, 161–166], we described studies of the association in detergent micelles of short, simple-sequence hydrophobic peptides modified from the sequence of the water-soluble, homodimeric coiled-coil GCN4-P1 peptide using the principle that the interiors of membrane proteins are similar to those of water-soluble proteins. Here, we discuss more quantitative aspects of the association equilibrium and compare the free energies of association of a number of mutant peptides designed to explore specific features responsible for the association.
Conference Article| August 01 2001
De novo design, synthesis and characterization of membrane-active peptides
J. D. Lear;
J. D. Lear 1
1The Johnson Research Foundation, Department of Biochemistry & Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, U.S.A.
1To whom correspondence should be addressed (e-mail email@example.com)
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J. D. Lear, H. Gratkowski, W. F. DeGrado; De novo design, synthesis and characterization of membrane-active peptides. Biochem Soc Trans 1 August 2001; 29 (4): 559–564. doi: https://doi.org/10.1042/bst0290559
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