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Changes in polypeptide conformer populations induced by the solvent environment
Author(s) -
Xu F.,
Cross T. A.
Publication year - 1998
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/(sici)1097-458x(199809)36:9<651::aid-omr341>3.0.co;2-6
Subject(s) - conformational isomerism , chemistry , solvent , dipole , solvent effects , membrane , dielectric , gramicidin , crystallography , stereochemistry , molecule , organic chemistry , biochemistry , physics , optoelectronics
Changes in the solvent dielectric properties are correlated with changes in polypeptide conformer populations. Gramicidin A, a peptide native to membrane environments, forms a variety of well defined dimeric conformations in relatively low dielectric organic solvents. However, changes in this environment lead to changes in the conformer populations with the lowest dielectric solvents favoring the conformers with the lowest net dipole moment. Such changes were characterized by cross‐peak intensities in GCOSY solution NMR spectra. In studying membrane‐bound polypeptides, it is very important to recognize that the structure is not dictated by just the amino acid sequence, but that the environment plays a very significant role in defining the polypeptide conformation. © 1998 John Wiley & Sons, Ltd.