Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: binding of phosphonamidate to the S₁'-pocket of thermolysin

Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: binding of phosphonamidate to the S₁'-pocket of thermolysin

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http://www.wikidata.org/entity/Q27663066
Experimental and computational active site mapping as a starting point to fragment-based lead discoveryWater makes the difference: rearrangement of water solvation layer triggers non-additivity of functional group contributions in protein-ligand bindingDissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysinMethyl, ethyl, propyl, butyl: futile but not for water, as the correlation of structure and thermodynamic signature shows in a congeneric series of thermolysin inhibitorsStructural Determinants of the Selectivity of 3-Benzyluracil-1-acetic Acids toward Human Enzymes Aldose Reductase and AKR1B10Thermodynamics of Water in an Enzyme Active Site: Grid-Based Hydration Analysis of Coagulation Factor Xa.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Water mediated ligand functional group cooperativity: the contribution of a methyl group to binding affinity is enhanced by a COO(-) group through changes in the structure and thermodynamics of the hydration waters of ligand-thermolysin complexes.Spatial Decomposition of Translational Water-Water Correlation Entropy in Binding Pockets.Molecular recognition in chemical and biological systems.Synthesis, Modelling, and Anticonvulsant Studies of New Quinazolines Showing Three Highly Active Compounds with Low Toxicity and High Affinity to the GABA-A Receptor.Enthalpic Breakdown of Water Structure on Protein Active-Site Surfaces.Design, Synthesis, Molecular Docking, and Anticancer Activity of Phthalazine Derivatives as VEGFR-2 Inhibitors.Solvent effects on ligand binding to a serine protease.Water-Restructuring Mutations Can Reverse the Thermodynamic Signature of Ligand Binding to Human Carbonic Anhydrase.Progesterone 5β-reductases/iridoid synthases (PRISE): gatekeeper role of highly conserved phenylalanines in substrate preference and trapping is supported by molecular dynamics simulations.
P2860

Displacement of disordered water molecules from hydrophobic pocket creates enthalpic signature: binding of phosphonamidate to the S₁'-pocket of thermolysin

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http://www.wikidata.org/entity/Q27663066
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2010 nî lūn-bûn
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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@ast
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@en
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@nl
type
label
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@ast
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@en
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@nl
prefLabel
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@ast
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@en
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P356
P1433
P1476
Displacement of disordered wat ...... the S₁'-pocket of thermolysin
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P2093
P304
P31
P356
10.1016/J.BBAGEN.2010.06.009
P407
P433
P478
P50
P577
P698
P921