Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy

FEBS Letters

Wishart, D.S.¹  Richards, F.M.¹  Sykes, B.D.² 

[1] Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA;MRC Group in Protein Structure and Function, Department of Biochemistry University of Alberta, AB, T6G 2H7, Canada

关键词: NMR: Chemical shift;    Secondary structure;    Protein structure;    Circular dichroism;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;    COSY;    two-dimensional correlated spectroscopy;    CD;    circular dichroisin spectroscopy;    IR;    infrared spectroscopy;   

DOI  :  10.1016/0014-5793(91)81155-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previous work by Wishart et al. (in press) and others [(1989) J. Magn. Reson. 83, 441–449; (1990) J. Magn. Reson. 9O, 165–176] has shown a strong tendency for protein secondary structure to be manifested in ¹H NMR chemical shifts. Based on these earlier results, two techniques have been developed for the quantification of secondary structure in proteins. Both methods allow for the rapid and accurate determination of the percent content of helix, coil. and β-strand based on the integration (or peak enumeration) of selected portions of either 1-D or 2-D ¹H NMR spectra. These new and very simple procedures have been found to compare quite favorably to other well established techniques for secondary structure determination such as CD, Raman and IR spectroscopy.

【 授权许可】

Unknown