title: Mosaic energy landscapes of liquids and the control of protein conformational dynamics by glass-forming solvents.
abstract: Using recent advances in the Random First-Order Transition (RFOT) Theory of glass-forming liquids, we explain how the molecular motions of a glass-forming solvent distort the protein's boundary and slave some of the protein's conformational motions. Both the length and time scales of the solvent imposed constraints are provided by the RFOT theory. Comparison of the protein relaxation rate to that of the solvent provides an explicit lower bound on the size of the conformational space explored by the protein relaxation. Experimental measurements of slaving of myoglobin motions indicate that a major fraction of functionally important motions have significant entropic barriers.
authors.affiliation: Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093-0371, USA. vas@mit.edu
authors.forename: Vassiliy
authors.initials: V
authors.lastname: Lubchenko
authors.forename: Peter G
authors.initials: PG
authors.lastname: Wolynes
authors.forename: Hans
authors.initials: H
authors.lastname: Frauenfelder
mesh_terms: D002627:Chemistry, Physical / Q000379:methods; D019277:Entropy; D005898:Glass / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D015233:Models, Statistical; D008968:Molecular Conformation; D009211:Myoglobin / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D009211:Myoglobin; D011506:Proteins; D012997:Solvents; D014867:Water