Increased protein backbone conformational entropy upon hydrophobic ligand binding

ŽÍDEK, Lukáš, Milos NOVOTNY and Martin J STONE. Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nature Structural Biology. New York: Nature America Inc., 1999, vol. 6, No 12, p. 1118-1121. ISSN 1072-8368.

Basic information

• Original name: Increased protein backbone conformational entropy upon hydrophobic ligand binding
• Authors: ŽÍDEK, Lukáš, Milos NOVOTNY and Martin J STONE.
• Edition: Nature Structural Biology, New York, Nature America Inc. 1999, 1072-8368.

Other information

• Type of outcome: Article in a journal
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 13.555
• Organization unit: Faculty of Science
• Keywords in English: N-15 NMR RELAXATION; NUCLEAR-MAGNETIC-RESONANCE; MODEL-FREE APPROACH; ORDER PARAMETERS; DYNAMICS; SPECTROSCOPY; RECOGNITION; ENERGY; DOMAIN; ENZYME
• Tags: DOMAIN, dynamics, energy, Enzyme, MODEL-FREE APPROACH, N-15 NMR RELAXATION, NUCLEAR-MAGNETIC-RESONANCE, ORDER PARAMETERS, recognition, spectroscopy

Abstract

For complexes between proteins and very small hydrophobic ligands, hydrophobic effects alone map 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 map represent a general mechanism to promote binding of very small ligands to macromolecules.