Physics – Chemical Physics
Scientific paper
1996-11-15
Phys. Rev. Letts. 77 (1996) 4966
Physics
Chemical Physics
Phys. Rev. Letts. (in press 1996), 3 pages, 3 figures
Scientific paper
10.1103/PhysRevLett.77.4966
An information theory model is used to construct a molecular explanation why hydrophobic solvation entropies measured in calorimetry of protein unfolding converge at a common temperature. The entropy convergence follows from the weak temperature dependence of occupancy fluctuations for molecular-scale volumes in water. The macroscopic expression of the contrasting entropic behavior between water and common organic solvents is the relative temperature insensitivity of the water isothermal compressibility. The information theory model provides a quantitative description of small molecule hydration and predicts a negative entropy at convergence. Interpretations of entropic contributions to protein folding should account for this result.
Garcia Angel E.
Garde Shekhar
Hummer Gerhard
Paulaitis Michael E.
Pratt Lawrence R.
No associations
LandOfFree
Origin of entropy convergence in hydrophobic hydration and protein folding does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.
If you have personal experience with Origin of entropy convergence in hydrophobic hydration and protein folding, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Origin of entropy convergence in hydrophobic hydration and protein folding will most certainly appreciate the feedback.
Profile ID: LFWR-SCP-O-352677