ISSN:
1573-4935
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The secondary chemical shift experienced by the1H-NMR resonances of the α C−H protons in proteins can be correlated with their backbone torsional angles ψ, which dictate the orientation of the α C−H proton to the adjacent carbonyl group. It is shown that α C−H protons present in β-sheet regions experience downfield secondary shifts , whereas those in α-helix regions experience upfield secondary shifts. The predictive use of this correlation in assignment studies is illustrated for the calcium-binding protein paravalbumin, for which a crystal structure is available, and troponin C, for which no crystallographic data are available.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01121955
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