Predicting conformational entropy of bond vectors in proteins by networks of coupled rotators.
In this article, a formal expression for the conformational entropy of a bond vector in a protein is derived using the networks of coupled rotators model for the description of internal dynamics. Analytical relationships between NMR order parameters and conformational entropies are derived, and the possibility to extract the latter from NMR experiments is discussed. These results are illustrated in the case of the calcium-binding protein calbindin.
Dhulesia
Anne
A
Department de Chimie, Associe au CNRS, Ecole Normale Superieure, 24, rue Lhomond, 75005 Paris, France.
Bodenhausen
Geoffrey
G
Abergel
Daniel
D
D000465:Algorithms; D003198:Computer Simulation; D019277:Entropy; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D011237:Predictive Value of Tests; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012399:Rotation
D011506:Proteins