Determination of Isoleucine Side-Chain Conformations in Ground and Excited States of Proteins from Chemical Shifts
Author:
Affiliation:
1. University of Toronto, Departments of Molecular Genetics, Biochemistry, and Chemistry, 1 King’s College Circle, Toronto, Ontario, Canada
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja102090z
Reference22 articles.
1. Protein structure determination from NMR chemical shifts
2. Consistent blind protein structure generation from NMR chemical shift data
3. Application of the random coil index to studying protein flexibility
4. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
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