Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.
A robust procedure for the determination of protein-backbone 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).
Salmon
Loïc
L
Protein Dynamics and Flexibility, Institute de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex, France.
Bouvignies
Guillaume
G
Markwick
Phineus
P
Lakomek
Nils
N
Showalter
Scott
S
Li
Da-Wei
DW
Walter
Korvin
K
Griesinger
Christian
C
Brüschweiler
Rafael
R
Blackledge
Martin
M
D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D025801:Ubiquitin / Q000737:chemistry*
D025801:Ubiquitin