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| - Mosaic Energy Landscapes of Liquids and the Control of Protein Conformational Dynamicsby Glass-Forming Solvents
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| - Using recent advances in the Random First-Order Transition (RFOT) Theory of glass-forming liquids, weexplain how the molecular motions of a glass-forming solvent distort the protein's boundary and slave someof the protein's conformational motions. Both the length and time scales of the solvent imposed constraintsare provided by the RFOT theory. Comparison of the protein relaxation rate to that of the solvent providesan explicit lower bound on the size of the conformational space explored by the protein relaxation. Experimentalmeasurements of slaving of myoglobin motions indicate that a major fraction of functionally important motionshave significant entropic barriers.
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