Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization. - Wikidata - awgldk - TriplyDB

Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization.

Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization.

http://www.wikidata.org/entity/Q34120049

about

Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity Quantifying the entropy of binding for water molecules in protein cavities by computing correlations Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility Incorporating replacement free energy of binding-site waters in molecular docking.Targeting Non-Catalytic Cysteine Residues Through Structure-Guided Drug Discovery Synchrotron X-ray footprinting as a method to visualize water in proteins.Thermodynamics of Water in an Enzyme Active Site: Grid-Based Hydration Analysis of Coagulation Factor Xa.Protein-spanning water networks and implications for prediction of protein-protein interactions mediated through hydrophobic effects.Overcoming Chemical, Biological, and Computational Challenges in the Development of Inhibitors Targeting Protein-Protein Interactions.Identification of protein-ligand binding sites by the level-set variational implicit-solvent approach A self-consistent phase-field approach to implicit solvation of charged molecules with Poisson-Boltzmann electrostatics.Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.BEDAM binding free energy predictions for the SAMPL4 octa-acid host challenge.A single glycine in extracellular loop 1 is the critical determinant for pharmacological specificity of dopamine D2 and D3 receptors.Improving the Resistance Profile of Hepatitis C NS3/4A Inhibitors: Dynamic Substrate Envelope Guided Design Heterogeneous Hydration of p53/MDM2 Complex.Approaches to efficiently estimate solvation and explicit water energetics in ligand binding: the use of WaterMap.Using crystallographic water properties for the analysis and prediction of lectin-carbohydrate complex structures.Benchmarking the thermodynamic analysis of water molecules around a model beta sheet.Probing water micro-solvation in proteins by water catalysed proton-transfer tautomerism.Enthalpic and Entropic Contributions to Hydrophobicity Solvation thermodynamic mapping of molecular surfaces in AmberTools: GIST.In silico studies of the properties of water hydrating a small protein.Quantum Mechanics Approaches to Drug Research in the Era of Structural Chemogenomics Assessing the accuracy of inhomogeneous fluid solvation theory in predicting hydration free energies of simple solutes.Combining solvent thermodynamic profiles with functionality maps of the Hsp90 binding site to predict the displacement of water molecules.Structured water molecules in the binding site of bromodomains can be displaced by cosolvent.Methods for Virtual Screening of GPCR Targets: Approaches and Challenges.Contributions of water transfer energy to protein-ligand association and dissociation barriers: Watermap analysis of a series of p38α MAP kinase inhibitors.The Role of Interfacial Water in Protein-Ligand Binding: Insights from the Indirect Solvent Mediated Potential of Mean Force.A Water-Bridged Cysteine-Cysteine Redox Regulation Mechanism in Bacterial Protein Tyrosine Phosphatases.Relationship between Solvation Thermodynamics from IST and DFT Perspectives.High end GPCR design: crafted ligand design and druggability analysis using protein structure, lipophilic hotspots and explicit water networks.The importance of hydration thermodynamics in fragment-to-lead optimization.Water Pharmacophore: Designing Ligands using Molecular Dynamics Simulations with Water.Dielectric response of frustrated water down to a single-molecule contribution Thermodynamic Profiling of Carbonic Anhydrase Inhibitors

P2860

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P2860

Thermodynamic analysis of water molecules at the surface of proteins and applications to binding site prediction and characterization.

http://www.wikidata.org/entity/Q34120049

description

2011 nî lūn-bûn

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2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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type

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Thermodynamic analysis of wate ...... ediction and characterization.

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Byungchan Kim

http://www.w3.org/2001/XMLSchema#string

Robert Abel

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Thijs Beuming

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Veerabahu Shanmugasundaram

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Woody Sherman

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Ye Che

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P2860

The RCSB Protein Data Bank: a redesigned query system and relational database based on the mmCIF schema

Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.

Bound water molecules and conformational stabilization help mediate an antigen-antibody association

Refinement of protein structures in explicit solvent

The Protein Data Bank: a computer-based archival file for macromolecular structures

Ligand binding to protein-binding pockets with wet and dry regions

Dominant forces in protein folding

Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes

Discovering high-affinity ligands for proteins: SAR by NMR

Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse

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871-883

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10.1002/PROT.23244

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3

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80

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