Calculation of entropy changes in biological processes: folding, binding, and oligomerization.
Changes in configurational entropy represent one of the major contributions to the thermodynamics of folding, binding, and oligomerization. Methods have been developed to estimate changes in the entropy of the backbone and side chains, and for the loss of translational entropy. These methods have been used in combination with empirical methods that provide estimates of the changes in entropy of solvation as well as estimates of the changes of enthalpy. The results of such calculations are in excellent agreement with experimentally observed values.
Amzel
L M
LM
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185, USA.
D019277:Entropy; D046911:Macromolecular Substances; D008433:Mathematics; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012984:Software; D012997:Solvents; D013816:Thermodynamics
D046911:Macromolecular Substances; D011506:Proteins; D012997:Solvents