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Mechanism of aldehyde oxidation catalyzed by horse liver alcohol dehydrogenase.
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Anticorrelated motions as a driving force in enzyme catalysis: the dehydrogenase reaction.
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Modeling of NAD+ analogues in horse liver alcohol dehydrogenase.
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Ligand-induced conformational changes enable intersubunit communications in D-dopachrome tautomerase.
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Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.
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Origin of Metal Cluster Tuning Enzyme Activity at the Bio-Nano Interface.
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An interdomain helix in IRE1α mediates the conformational change required for the sensor's activation.
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Cleavage, Downregulation, and Aggregation of Serum Amyloid A.
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Immobilization of the N-terminal helix stabilizes prefusion paramyxovirus fusion proteins.
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1
All-atom empirical potential for molecular modeling and dynamics studies of proteins.
J Phys Chem B. 1998 Apr 30;102(18):3586-616. doi: 10.1021/jp973084f.
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A link between protein structure and enzyme catalyzed hydrogen tunneling.
Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12797-802. doi: 10.1073/pnas.94.24.12797.
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Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution.
J Mol Biol. 1976 Mar 25;102(1):27-59. doi: 10.1016/0022-2836(76)90072-3.

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