TY - JOUR
T1 - Protein conformational flexibility from structure-free analysis of NMR dipolar couplings
T2 - Quantitative and absolute determination of backbone motion in ubiquitin
AU - Salmon, Loïe
AU - Bouvignies, Guillaume
AU - Markwick, Phineus
AU - Lakomek, Nils
AU - Showalter, Scott
AU - Li, Da Wei
AU - Walter, Korvin
AU - Griesinger, Christian
AU - Brüschweiler, Rafael
AU - Blackledge, Martin
PY - 2009/5/25
Y1 - 2009/5/25
N2 - A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).
AB - A robust procedure for the determination of proteinbackbone motions on time scales of pico- to milliseconds directly from residual dipolar couplings has been developed that requires no additional scaling relative to external references. The results for ubiquitin (blue in graph: experimental N HN order parameters) correspond closely to the amplitude, nature, and distribution of motion found in a 400 ns molecular-dynamics trajectory of ubiquitin (red).
UR - https://www.scopus.com/pages/publications/70349784868
UR - https://www.scopus.com/pages/publications/70349784868#tab=citedBy
U2 - 10.1002/anie.200900476
DO - 10.1002/anie.200900476
M3 - Article
C2 - 19415702
AN - SCOPUS:70349784868
SN - 1433-7851
VL - 48
SP - 4154
EP - 4157
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 23
ER -