Nuclear Overhauser effects as probes of peptide structure. A diagnostic for left-handed helical conformations.

Abstract:

:The conformational dependence of the interresidue interproton distances in peptides, C alpha H ... Ni + 1 H and NiH ... Ni + 1 H, have been used to identify zones of sterically allowed phi, psi space, where both distances are less than 3A and expected to yield nuclear Overhauser effects (NOEs). L-residues in left-handed helical conformations are expected to yield both interresidue NOEs and also an appreciable intraresidue NiH----C alpha iH NOE. The effect of cutoff distances has been evaluated. Experimental results on three model peptides illustrate the utility of these NOEs in identifying L-residues at the i + 2 position of Type II and I' beta-turns. Simultaneous observation of both interresidue NOEs may also be indicative of conformational heterogeneity in specific cases, as illustrated for a single residue in a decapeptide.

authors

Ramakrishnan C,Sukumar M,Balaram P

doi

10.1016/0006-291x(87)90501-8

subject

Has Abstract

pub_date

1987-12-31 00:00:00

pages

953-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(87)90501-8

journal_volume

149

pub_type

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