Thermodynamic analysis of protein unfolding in aqueous solutions as a multisite reaction of protein with water and solute molecules.
Thermal unfolding of ribonuclease A, lysozyme, and chymotrypsinogen A was analyzed as a multisite reaction of a protein molecule with water and solute molecules. The protein unfolding process in various solutions of sugars and denaturants was described well by the van't Hoff equation. The reciprocal form of the Wyman-Tanford equation, which describes the unfolded-to-folded protein ratio as a function of water activity, was successfully applied to obtain a good linear relationship. From this analysis, the role of water activity on protein stability was clearly explained and the contributions of hydration and solute binding to protein molecule were separately discussed in protein unfolding. General solution for the free energy of protein stability was obtained as a simple function of solute concentration.
Miyawaki
Osato
O
Department of Food Science, Ishikawa Prefectural University, Nonoichi, Ishikawa 921-8836, Japan. osato@ishikawa-pu.ac.jp
D000465:Algorithms; D002919:Chymotrypsinogen / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
D014867:Water; D002919:Chymotrypsinogen; D012259:Ribonuclease, Pancreatic; D009113:Muramidase