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Simple techniques for the quantification of protein secondary structure by 1 H NMR spectroscopy
Author(s) -
Wishart D.S.,
Sykes B.D.,
Richards F.M.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81155-2
Subject(s) - chemistry , protein secondary structure , nuclear magnetic resonance spectroscopy , spectroscopy , raman spectroscopy , chemical shift , analytical chemistry (journal) , crystallography , physics , chromatography , stereochemistry , optics , biochemistry , quantum mechanics
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 1 H 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 1 H 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.