Although the nature of solvent-protein interactions is generally weak and non-specific, addition of cosolvents such as denaturants and osmolytes strengthens protein-protein interactions for some proteins, whereas it weakens protein-protein interactions for others. This is exemplified by the puzzling observation that addition of glycerol oppositely affects the association constants of two antibo...

Discrete nature of water plays critical role in protein folding and thermodynamics. Explicit all-atom modeling of solvent severely limits the length and time scales of molecular dynamics simulations of protein. In this project, we evaluated accuracy and computational efficiency of four different solvent models, all-atom solvent models ( SPC/E and TIP3P ), Generalized Born Implicit Solvent, and ...

This research focuses on the effects of water in a solvent on a synthetic process of a Grignard reagent which is common in organic synthesis and triggered an accident in Japan. For the measurement, a hermetically sealed apparatus was prepared to fit a small-scaled reaction calorimeter. The experimental results revealed that the induction period appeared as the water content in the solvent incre...

The phenomenological model of Khossravi and Connors (1992) has been adopted to calculate the electrophoretic mobility of drugs at different concentrations of solvents in a binary mixture. The accuracy and predictability of the model have been evaluated employing 14 experimental data sets by using average percentage mean deviation (APMD). The obtained APMD for correlative and predictive studies ...

The excited-state lifetime of the metal-to-ligand charge-transfer (MLCT) excited state or states of Ru(bpy)3Z+ has been measured in a series of solvents a t a series of temperatures. The data can be fit to the equation r(T)-' = k + k"' exp [ (AE'/k,T)] where k is the sum of the radiative ( k , ) and nonradiative (k, ,) rate constants for decay of the MLCT state(s) and the temperature-dependent ...

Characterization of solvent preferences of proteins is essential to the understanding of solvent effects on protein structure and stability. Although it is generally believed that solvent preferences at distinct loci of a protein surface may differ, quantitative characterization of local protein solvation has remained elusive. In this study, we show that local solvation preferences can be quant...

Several simulation methods are currently in use to study peptide and protein folding. They can be classified in three groups depending on how the solvent is treated. At the simplest level, the solvent is ignored. At a second level, solvent effects are implicitly represented in the atomic interaction function. At the third level, solvent degrees of freedom are treated explicitly. We have perform...