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Published on: January 26, 2016
De novo design, synthesis and characterization of membrane-active peptides
J D Lear1, H Gratkowski, W F DeGrado
1The Johnson Research Foundation, Department of Biochemistry & Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA. lear@mail.med.upenn.edu
Abstract:
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.
