PMID: 9175271Apr 22, 1997Paper

Equilibrium and non-equilibrium conformations of peptides in lipid bilayers

Biophysical Chemistry
N BodenP F Knowles

Abstract

A synthetic, hydrophobic, 27-amino-acid-residue peptide 'K27', modelled on the trans-membrane domain of the slow voltage-gated potassium channel, IsK, has been incorporated into a lipid bilayer and its conformational properties studied using FT-IR spectroscopy. The conformation following reconstitution is found to be dependent on the nature of the solvent employed. When the reconstitution is conducted by solvent evaporation from a methanol solution, aggregates comprised of beta-strands are stabilised and their concentration is essentially invariant with time. By contrast, when trifluoroethanol is used, the initial conformation of the peptide is alpha-helical. This then relaxes to an equilibrium state between alpha-helices and beta-strands. The alpha-helix-to beta-strand conversion rate is relatively slow, and this allows the kinetics to be studied by FT-IR spectroscopy. The reverse process is much slower but again can be demonstrated by FT-IR. Thus, it appears that a true equilibrium structure can only be achieved by starting with peptide in the alpha-helical conformation. We believe this result should be of general validity for hydrophobic peptide reconstitution. The implications for conformational changes in membrane proteins...Continue Reading

References

May 1, 1990·Biochemistry·J L Popot, D M Engelman
Dec 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·K M PanF E Cohen

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Citations

Aug 6, 2018·Biophysical Journal·Mike ZhangHelgi I Ingólfsson

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