Entropy in protein folding and in protein—protein interactions

• Published in: Current opinion in structural biology Vol. 7; no. 2; pp. 215 - 221
• Main Authors: Brady, G Patrick, Sharp, Kim A
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01-04-1997
• Subjects: Algorithms; Databases, Factual; Entropy; Protein Binding; Protein Conformation; Solvents; TI thermodynamic integration; eu entropy units; SAS solvent accessible surface
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/S0959-440X(97)80028-0

The reduction of conformational entropy is a major barrier that has to be overcome in protein folding and binding. Changes in solvent entropy are also a major factor. Recent advances include clarification of the fundamental issues concerning the separation of entropy into components, the treatment of association entropy in binding, and the role of size and shape effects in solvation entropy. Advances in the application of entropy calculations include an emerging consensus for estimates of backbone and sidechain entropy loss in protein folding via use of numerically intensive methods for sampling, and use of the expanding protein-structure database.