Search:
Computing and Library Services - delivering an inspiring information environment

Strong Solute−Solute Dispersive Interactions in a Protein−Ligand Complex

Malham, Richard, Johnstone, Sarah, Bingham, Richard, Barratt, Elizabeth, Phillips, Simon E. V., Laughton, Charles A. and Homans, Steve W. (2005) Strong Solute−Solute Dispersive Interactions in a Protein−Ligand Complex. Journal of the American Chemical Society, 127 (48). pp. 17061-17067. ISSN 1520-5126

Metadata only available from this repository.

Abstract

The contributions of solute−solute dispersion interactions to binding thermodynamics have generally been thought to be small, due to the surmised equality between solute−solvent dispersion interactions prior to the interaction versus solute−solute dispersion interactions following the interaction. The thermodynamics of binding of primary alcohols to the major urinary protein (MUP-I) indicate that this general assumption is not justified. The enthalpy of binding becomes more favorable with increasing chain length, whereas the entropy of binding becomes less favorable, both parameters showing a linear dependence. Despite the hydrophobicity of the interacting species, these data show that binding is not dominated by the classical hydrophobic effect, but can be attributed to favorable ligand−protein dispersion interactions.

Item Type: Article
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Schools: School of Applied Sciences
Related URLs:
Depositing User: Graham Stone
Date Deposited: 09 Oct 2009 10:02
Last Modified: 09 Oct 2009 10:02
URI: http://eprints.hud.ac.uk/id/eprint/5828

Item control for Repository Staff only:

View Item

University of Huddersfield, Queensgate, Huddersfield, HD1 3DH Copyright and Disclaimer All rights reserved ©