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

Článek v odborném periodiku

Confidentiality degree

není předmětem státního či obchodního tajemství

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

V originále

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.