Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function.
Wand
A J
AJ
The Johnson Research Foundation & Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. wand@mail.med.upenn.edu
D000494:Allosteric Regulation; D002384:Catalysis; D019277:Entropy; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D009038:Motion; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D004798:Enzymes; D011506:Proteins