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

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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:	Author
Depositing User:	Graham Stone
Date Deposited:	09 Oct 2009 09:02
Last Modified:	28 Aug 2021 10:51
URI:	http://eprints.hud.ac.uk/id/eprint/5828

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