Ligand configurational entropy and protein binding. - Test2 - elhamkhani - TriplyDB

Ligand configurational entropy and protein binding.

Ligand configurational entropy and protein binding.

http://www.wikidata.org/entity/Q35607011

about

Correlation as a determinant of configurational entropy in supramolecular and protein systems Water in cavity-ligand recognition.Druggability Assessment of Allosteric Proteins by Dynamics Simulations in the Presence of Probe Molecules Charting a Path to Success in Virtual Screening HIV-1 Protease Inhibitors from Inverse Design in the Substrate Envelope Exhibit Subnanomolar Binding to Drug-Resistant Variants Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3 Structure of catalytic domain of Matriptase in complex with Sunflower trypsin inhibitor-1 A detailed thermodynamic profile of cyclopentyl and isopropyl derivatives binding to CK2 kinase Prediction of cyclin-dependent kinase 2 inhibitor potency using the fragment molecular orbital method AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading Patient-specific simulation as a basis for clinical decision-making Theory of free energy and entropy in noncovalent binding Develop and test a solvent accessible surface area-based model in conformational entropy calculations Grid inhomogeneous solvation theory: hydration structure and thermodynamics of the miniature receptor cucurbit[7]uril Toward accurate microscopic calculation of solvation entropies: extending the restraint release approach to studies of solvation effects Efficient Computation of Small-Molecule Configurational Binding Entropy and Free Energy Changes by Ensemble Enumeration Configurational entropy in protein-peptide binding: computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptide Absolute Single-Molecule Entropies from Quasi-Harmonic Analysis of Microsecond Molecular Dynamics: Correction Terms and Convergence Properties Estimating absolute configurational entropies of macromolecules: the minimally coupled subspace approach Equilibrium sampling in biomolecular simulations Energetics of Ortho-7 (oxime drug) translocation through the active-site gorge of tabun conjugated acetylcholinesterase Extraction of configurational entropy from molecular simulations via an expansion approximation A dock and coalesce mechanism driven by hydrophobic interactions governs Cdc42 binding with its effector protein ACK Prediction of the water content in protein binding sites Event detection and sub-state discovery from biomolecular simulations using higher-order statistics: application to enzyme adenylate kinase.Dominant Alcohol-Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism Toward a molecular understanding of the interaction of dual specificity phosphatases with substrates: insights from structure-based modeling and high throughput screening.Molecular determinants of juvenile hormone action as revealed by 3D QSAR analysis in Drosophila.Organised chaos: entropy in hybrid inorganic-organic systems and other materials Binding free energy landscape of domain-peptide interactions.The interprotein scoring noises in glide docking scores.Modeling the pharmacodynamics of passive membrane permeability Large scale affinity calculations of cyclodextrin host-guest complexes: Understanding the role of reorganization in the molecular recognition process.Virtual screening of integrase inhibitors by large scale binding free energy calculations: the SAMPL4 challenge.Amyloid-β peptide structure in aqueous solution varies with fragment size.The Binding Energy Distribution Analysis Method (BEDAM) for the Estimation of Protein-Ligand Binding Affinities.Novel analogues of the therapeutic complement inhibitor compstatin with significantly improved affinity and potency.VP40 of the Ebola Virus as a Target for EboV Therapy: Comprehensive Conformational and Inhibitor Binding Landscape from Accelerated Molecular Dynamics.Free-energy calculations for semi-flexible macromolecules: applications to DNA knotting and looping.Empirical entropic contributions in computational docking: evaluation in APS reductase complexes.

P2860

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P2860

Ligand configurational entropy and protein binding.

http://www.wikidata.org/entity/Q35607011

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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2007年论文

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2007年论文

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name

Ligand configurational entropy and protein binding.

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Ligand configurational entropy and protein binding.

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Ligand configurational entropy and protein binding.

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Ligand configurational entropy and protein binding.

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Ligand configurational entropy and protein binding.

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Ligand configurational entropy and protein binding.

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PNAS.0610494104

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Ligand configurational entropy and protein binding.

@en

P2093

Chia-en A Chang

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

Michael K Gilson

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

Wei Chen

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

P2860

The Protein Data Bank

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

Ligand efficiency: a useful metric for lead selection

The statistical-thermodynamic basis for computation of binding affinities: a critical review

On the calculation of absolute macromolecular binding free energies

Revisiting free energy calculations: a theoretical connection to MM/PBSA and direct calculation of the association free energy

Calculation of cyclodextrin binding affinities: energy, entropy, and implications for drug design.

Configurational entropy of native proteins.

The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure.

Further development and validation of empirical scoring functions for structure-based binding affinity prediction.

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1534-1539

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scholarly article

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10.1073/PNAS.0610494104

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5

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104

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2007-01-22T00:00:00Z

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6561436

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1780070

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