Simple techniques for the quantification of protein secondary structure by 1H NMR spectroscopy.
Previous work by Wishart et al. (in press) and others [(1989) J. Magn. Reson. 83, 441-449; (1990) J. Magn. Reson. 90, 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 beta-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.
Wishart
D S
DS
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Sykes
B D
BD
Richards
F M
FM
D000818:Animals; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D051381:Rats; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D014961:X-Ray Diffraction
D010455:Peptides