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 1520-5126Metadata only available from this repository.
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.
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Schools:||School of Applied Sciences|
|Depositing User:||Graham Stone|
|Date Deposited:||09 Oct 2009 09:02|
|Last Modified:||09 Oct 2009 09:02|
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