Protein folding, stability, and solvation structure in osmolyte solutions.
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.
Rösgen
Jörg
J
Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555-1052, USA. jorosgen@utmb.edu
Pettitt
B Montgomery
BM
Bolen
David Wayne
DW
D001703:Biophysics / Q000379:methods*; D003593:Cytoplasm / Q000378:metabolism; D015233:Models, Statistical; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D055672:Static Electricity; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D011506:Proteins; D014867:Water