On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation. Issue 1 (February 1996)

• Record Type: Journal Article
• Authors: Singha, Netai C.; Surolia, Namita; Surolia, A.
• Is Part Of: Bioscience reports. Volume 16:Issue 1(1996)
• Page Start: 1
• Page End: 10
• Publication Date: 1996-02
• Subjects: Buried site -- ligand -- protein-ligand complex -- thermodynamic parameters; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1007/BF01200996
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : Prediction of thermodynamic parameters of protein-protein and antigen-antibody complex formation from high resolution structural parameters has recently received much attention, since an understanding of the contributions of different fundamental processes like hydrophobic interactions, hydrogen bonding, salt bridge formation, solvent reorganization etc. to the overall thermodynamic parameters and their relations with the structural parameters would lead to rational drug design. Using the results of the dissolution of hydrocarbons and other model compounds the changes in heat capacity (ΔCp ), enthalpy (ΔH) and entropy (ΔS) have been empirically correlated with the polar and apolar surface areas buried during the process of protein folding/unfolding and protein-ligand complex formation. In this regard, the polar and apolar surfaces removed from the solvent in a protein-ligand complex have been calculated from the experimentally observed values of changes in heat capacity (ΔCp ) and enthalpy (ΔH) for protein-ligand complexes for which accurate thermodynamic and high resolution structural data are available, and the results have been compared with the x-ray crystallographic observations. Analyses of the available results show poor correlation between the thermodynamic and structural parameters. Probable reasons for this discrepancy are mostly related with the reorganization of water accompanying the reaction which is indeed proven by the analyses of the energetics of the binding of the wheat germ agglutinin to oligosaccharides.