Journal article

The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG

KW Plaxco, CJ Morton, SB Grimshaw, JA Jones, M Pitkeathly, ID Campbell, CM Dobson

Journal of Biomolecular NMR | KLUWER ACADEMIC PUBL | Published : 1997

Abstract

The effects of the commonly used denaturant guanidine hydrochloride(GuHCl) on the random coil conformations and NMR chemical shifts of theproteogenic amino acids have been characterized using the peptide seriesAc-Gly-Gly-X-Gly-Gly-NH(2). The phi angle-sensitive couplingconstants, ROESY cross peak intensities and proline cis-trans isomerratios of a representative subset of these peptides are unaffected by GuHCl,which suggests that the denaturant does not significantly perturb intrinsicbackbone conformational preferences. A set of(3)J(HNHalpha) values is presented which agreewell with predictions of recently developed models of the random coil. Wehave also measured the chemical shifts of all 2..

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University of Melbourne Researchers