How Much Binding Affinity Can be Gained by Filling a Cavity? - Test2 - elhamkhani - TriplyDB

How Much Binding Affinity Can be Gained by Filling a Cavity?

How Much Binding Affinity Can be Gained by Filling a Cavity?

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Finding a better path to drug selectivity A detailed thermodynamic profile of cyclopentyl and isopropyl derivatives binding to CK2 kinase Interfacial Cavity Filling To Optimize CD4–Mimetic Miniprotein Interactions with HIV-1 Surface Glycoprotein Protein–ligand interactions: Probing the energetics of a putative cation–π interaction Ligand binding analysis and screening by chemical denaturation shift Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Protocol for rational design of covalently interacting inhibitors.Synthetic, structural mimetics of the β-hairpin flap of HIV-1 protease inhibit enzyme function.Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.Redesigning protein cavities as a strategy for increasing affinity in protein-protein interaction: interferon- γ receptor 1 as a model.Enthalpy screen of drug candidates.Characterization of the flexibility of the peripheral stalk of prokaryotic rotary A-ATPases by atomistic simulations.PHOENIX: a scoring function for affinity prediction derived using high-resolution crystal structures and calorimetry measurements Stilbene Boronic Acids Form a Covalent Bond with Human Transthyretin and Inhibit Its Aggregation.Impact of binding mechanism on selective inhibition of histone deacetylase isoforms.

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P2860

How Much Binding Affinity Can be Gained by Filling a Cavity?

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2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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How Much Binding Affinity Can be Gained by Filling a Cavity?

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How Much Binding Affinity Can be Gained by Filling a Cavity?

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J.1747-0285.2009.00921.X

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Chemical Biology and Drug Design

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Eduardo E Chufan

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Ernesto Freire

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Koushi Hidaka

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Virginie Lafont

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Compensating enthalpic and entropic changes hinder binding affinity optimization

Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors

Automated protein model building combined with iterative structure refinement

Macromolecular TLS refinement in REFMAC at moderate resolutions

UCSF Chimera--a visualization system for exploratory research and analysis

The interpretation of protein structures: estimation of static accessibility

Shape complementarity at protein/protein interfaces

Refinement of macromolecular structures by the maximum-likelihood method

The CCP4 suite: programs for protein crystallography

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