| Title: | Increased protein backbone conformational entropy upon hydrophobic ligand binding |
| Author(s): | Zidek L; Novotny MV; Stone MJ; |
| Address: | "Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA" |
| ISSN/ISBN: | 1072-8368 (Print) 1072-8368 (Linking) |
| Abstract: | "For complexes between proteins and very small hydrophobic ligands, hydrophobic effects alone may be insufficient to outweigh the unfavorable entropic terms resulting from bimolecular association. NMR relaxation experiments indicate that the backbone flexibility of mouse major urinary protein increases upon binding the hydrophobic mouse pheromone 2-sec-butyl-4,5-dihydrothiazole. The associated increase in backbone conformational entropy of the protein appears to make a substantial contribution toward stabilization of the protein-pheromone complex. This term is likely comparable in magnitude to other important free energy contributions to binding and may represent a general mechanism to promote binding of very small ligands to macromolecules" |
| Keywords: | "Animals *Entropy Kinetics Ligands Mice Models, Molecular Molecular Weight Nuclear Magnetic Resonance, Biomolecular Pheromones/chemistry/metabolism Protein Binding Protein Structure, Secondary Proteins/*chemistry/*metabolism Static Electricity Stereoisomer;" |
| Notes: | "MedlineZidek, L Novotny, M V Stone, M J eng Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1999/12/03 Nat Struct Biol. 1999 Dec; 6(12):1118-21. doi: 10.1038/70057" |
