Increased protein backbone conformational entropy upon hydrophobic ligand binding

ŽÍDEK, Lukáš, Milos NOVOTNY a Martin J STONE. Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nature Structural Biology. New York: Nature America Inc., 1999, roč. 6, č. 12, s. 1118-1121. ISSN 1072-8368.

Základní údaje

Originální název

Increased protein backbone conformational entropy upon hydrophobic ligand binding

Autoři

ŽÍDEK, Lukáš, Milos NOVOTNY a Martin J STONE

Vydání

Nature Structural Biology, New York, Nature America Inc. 1999, 1072-8368

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Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 13.555

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

N-15 NMR RELAXATION; NUCLEAR-MAGNETIC-RESONANCE; MODEL-FREE APPROACH; ORDER PARAMETERS; DYNAMICS; SPECTROSCOPY; RECOGNITION; ENERGY; DOMAIN; ENZYME

Štítky

DOMAIN, dynamics, energy, Enzyme, MODEL-FREE APPROACH, N-15 NMR RELAXATION, NUCLEAR-MAGNETIC-RESONANCE, ORDER PARAMETERS, recognition, spectroscopy

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Anotace

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.