Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions

A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis

(2011) G. Bhabha et al.   SCIENCE

Protein dynamics and enzyme catalysis: Insights from simulations

(2010) John D. McGeagh et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

The role of conformational entropy in molecular recognition by calmodulin

(2010) Michael S Marlow et al.   Nature Chemical Biology

Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization

(2010) S. C. L. Kamerlin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hidden alternative structures of proline isomerase essential for catalysis

(2009) James S. Fraser et al.   NATURE

Enzyme millisecond conformational dynamics do not catalyze the chemical step

(2009) A. V. Pisliakov et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The energetics of the primary proton transfer in bacteriorhodopsin revisited: It is a sequential light-induced charge separation after all

(2008) Sonja Braun-Sand et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS