Journal of Biomolecular NMR

, Volume 1, Issue 1, pp 99–104

An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the α-carbon of the preceding residue in uniformly15N/13C enriched proteins

Authors

  • Ad Bax
    • Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney DiseasesNational Institutes of Health
  • Mitsuhiko Ikura
    • Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney DiseasesNational Institutes of Health
Short Communications

DOI: 10.1007/BF01874573

Cite this article as:
Bax, A. & Ikura, M. J Biomol NMR (1991) 1: 99. doi:10.1007/BF01874573

Summary

A 3D NMR technique is described which correlates the amide proton and nitrogen resonances of an amino acid residue with the Cα chemical shift of its preceding residue. The technique uses a relay mechanism, transferring magnetization from15N to13Cα via the intervening carbonyl nucleus. This method for obtaining sequential connectivity is less sensitive to large line widths than the alternative HNCA experiment. The technique is demonstrated for the protein calmodulin, complexed with a 26 amino acid fragment of skeletal muscle myosin light chain kinase.

Keywords

3D NMRTriple resonance assignmentHeteronuclearCalmodulin

Abbreviations

CaM

Calmodulin

HCACO

α-proton to α-carbon to carbonyl correlation

H(CA)NHN

α-proton (via α-carbon) to nitrogen to amide proton correlation

HMQC

heteronuclear multiple quantum correlation

HNCA

amide proton to nitrogen to C α-carbon correlation

M13

a 26-residue fragment of the CaM-binding domain of skeletal muscle myosin light chain kinase comprising residues 577–602.

Copyright information

© ESCOM Science Publishers B.V. 1991