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

• Published in: FEBS letters 1991-11, Vol.293 (1), p.72-80
• Main Authors: Wishart, D.S., Sykes, B.D., Richards, F.M.
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; circular dichroisin spectroscopy; Circular Dichroism; COSY; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; infrared spectroscopy; Magnetic Resonance Spectroscopy - methods; NMR; NMR: Chemical shift, Secondary structure; NOE; nuclear magnetic resonance; nuclear Overhauser effect; Peptides - chemistry; Protein Conformation; Protein structure; Proteins; Rats; Spectrophotometry, Infrared; Spectrum Analysis, Raman; two-dimensional correlated spectroscopy; X-Ray Diffraction
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(91)81155-2

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.