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


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