PROTEIN FLEXIBILITY IN AQUEOUS AND NONAQUEOUS SOLUTIONS

Herein we present the results of molecular dynamics simulations of a protein in an organic solvent. Our results show that while the amino acid side chains are more flexible in water, there is only a very small difference in backbone flexibility between protein in chloroform and protein in water. We propose that the major difference between the two solvent environments is the preferred orientations of the amino acid side chains. These results aid in the understanding of experimental observations and offer important insights for protein engineering in nonaqueous media.