Analysis of asymmetry in the distribution of helical residues in peptides by 1H nuclear magnetic resonance

M. I. Liff, P. C. Lyu, N. R. Kallenbach

Research output: Contribution to journalArticle

Abstract

Peptides that assume full or partial helical structure in aqueous solution have provided useful models for investigating the determinants of α-helical structure. Circular dichroism (CD) spectroscopy, the usual measure of helicity, affords an estimate of the mean helix content when calibrated against suitable standards. Analysis of these systems by means of 1H NMR makes it possible to determine precisely the location and extent of helix structure in a chain. NMR criteria for identifying helical domains include the following: NOE's between adjacent NH protons and between an NH proton at position i and the Cα proton at i + 3; values of the three-bond coupling constants 3JαN; and the relative chemical shift of the Cα protons. Application of these criteria to members of the series of partially helical synthetic peptides, succinylTyrSerGlu4Lys4XXXGlu4Lys 4NH2, in which sets of three amino acids are inserted between blocks of glutamic acid and lysine side chains, shows that the helix is located preferentially near the N terminus in chains with the central substitution Ala3,Leu3, as well as in the parent species lacking any substitution. The degree of helicity rises sharply at the N terminus to a maximum near residue 8 and diminishes gradually from Glu14 to the C terminus. Application of the NMR criteria to the peptide containing Gly3 reveals very little helical structure in this peptide. These results suggest that helix formation in short chains does not conform to an all-or-none reaction.

Original languageEnglish (US)
Pages (from-to)1014-1019
Number of pages6
JournalJournal of the American Chemical Society
Volume113
Issue number3
StatePublished - Jan 30 1991

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Peptides
Protons
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Substitution reactions
Circular dichroism spectroscopy
Chemical shift
Circular Dichroism
Systems Analysis
Lysine
Amino acids
Glutamic Acid
Spectrum Analysis
Amino Acids
Acids

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Analysis of asymmetry in the distribution of helical residues in peptides by 1H nuclear magnetic resonance. / Liff, M. I.; Lyu, P. C.; Kallenbach, N. R.

In: Journal of the American Chemical Society, Vol. 113, No. 3, 30.01.1991, p. 1014-1019.

Research output: Contribution to journalArticle

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