Slaving: Solvent fluctuations dominate protein dynamics and functions

By P. Fenimore, H. Frauenfelder, B. McMahon, F. Parak. Proceedings of the National Academy of Sciences of the United States of America, 2002

606 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Water mediation in protein folding and molecular recognition. (2006, background): “There is high coupling between the protein motions and water dynamics, and it has been suggested that fluctuations of the hydration water can slave the protein dynamics and thus affect its function (2, 48, 99).”
Dynamic personalities of proteins (2007, background): “Subsequent studies on myoglobin led to the idea that substates are in thermal equilibrium and that both solven”
A unified model of protein dynamics (2009, background): “Protein motions that involve shape changes, such as folding or opening of a gate to permit the entry and exit of ligands, are slaved to the f luctuations in the bulk solvent (2, 3).”