Conformational Entropy of FK506 Binding to FKBP12 Determined by Nuclear Magnetic Resonance Relaxation and Molecular Dynamics Simulations

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Date: Mar. 6, 2018
From: Biochemistry(Vol. 57, Issue 9)
Publisher: American Chemical Society
Document Type: Report
Length: 42 words

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Abstract :

The article reports protein conformational entropy contributions to free energy of ligand binding FKBP12 (FK506 binding protein 12 kDa) drug target. Topics include molecular dynamics simulations delicate dependence on drug interactions determined by nuclear magnetic resonance relaxation associated with isothermal titration calorimetry.

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Gale Document Number: GALE|A534790699