Accurate Random Coil Chemical Shifts from an Analysis of Loop Regions in Native States of Proteins
Author:
Affiliation:
1. Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., and European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge CB10 1SD, U.K.
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja904937a
Reference19 articles.
1. Sequence-Corrected 15N "Random Coil" Chemical Shifts
2. Sequence-Dependent Correction of Random Coil NMR Chemical Shifts
3. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
4. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts
5. Intrinsically unstructured proteins and their functions
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