Predicting the energetics of osmolyte-induced protein folding/unfolding.
A primary thermodynamic goal in protein biochemistry is to attain predictive understanding of the detailed energetic changes that are responsible for folding/unfolding. Through use of recently determined free energies of side-chain and backbone transfer from water to osmolytes and Tanford's transfer model, we demonstrate that the long-sought goal of predicting solvent-dependent cooperative protein folding/unfolding free-energy changes (m values) can be achieved. Moreover, the approach permits dissection of the folding/unfolding free-energy changes into individual contributions from the peptide backbone and residue side chains.
Auton
Matthew
M
Department of Human Biological Chemistry, University of Texas Medical Branch, 301 University Boulevard, 5.154 Medical Research Building, Galveston, TX 77555-1052, USA.
Bolen
D Wayne
DW
D008962:Models, Theoretical; D009994:Osmolar Concentration; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012997:Solvents / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins; D012997:Solvents