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Protein Folding, Stability, and Solvation Structure in Osmolyte Solutions

Jörg Rösgen ^* , B. Montgomery Pettitt  and David Wayne Bolen ^*

^* Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas 77555-1052; and Department of Chemistry, University of Houston, Houston, Texas 77204-5003

Correspondence: Address reprint requests to Jörg Rösgen, Dept. of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555-1052. Tel.: 409-772-0968; Fax: 409-747-4751; E-mail: jorosgen{at}utmb.edu.

An understanding of the impact of the crowded conditions in the cytoplasm on its biomolecules is of clear importance to biochemical, medical, and pharmaceutical science. Our previous work on the use of small biochemical compounds to crowd protein solutions indicates that a quantitative description of their nonideal behavior is possible and straightforward. Here, we show the structural origin of the nonideal solution behavior. We discuss the consequences of these findings regarding protein folding stability and solvation in crowded solutions through a structural analysis of the m-value or the change in free-energy difference of a macromolecule in solution with respect to the concentration of a third component.

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