Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding - Wikidata - wikimedia - TriplyDB

Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding

Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding

http://www.wikidata.org/entity/Q34145063

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C-terminal substitution of MDM2 interacting peptides modulates binding affinity by distinctive mechanisms Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase High-throughput analysis of peptide-binding modules Energetics of Ortho-7 (oxime drug) translocation through the active-site gorge of tabun conjugated acetylcholinesterase Interolog interfaces in protein-protein docking Relative Binding Enthalpies from Molecular Dynamics Simulations Using a Direct Method.Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design.Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 Protease.A simplified confinement method for calculating absolute free energies and free energy and entropy differences.Configurational space discretization and free energy calculation in complex molecular systems.Detection of long-range concerted motions in protein by a distance covariance.Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.Limiting assumptions in structure-based design: binding entropy.A prospective overview of the essential requirements in molecular modeling for nanomedicine design.Natural Products and Their Mimics as Targets of Opportunity for Discovery.Evaluating the dynamics and electrostatic interactions of folded proteins in implicit solvents.Deletion of the carboxyl-terminal residue disrupts the amino-terminal folding, self-association, and thermal stability of an amphipathic antimicrobial peptide.

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P2860

Constraining binding hot spots: NMR and molecular dynamics simulations provide a structural explanation for enthalpy-entropy compensation in SH2-ligand binding

http://www.wikidata.org/entity/Q34145063

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին 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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name

Constraining binding hot spots ...... ensation in SH2-ligand binding

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Constraining binding hot spots ...... ensation in SH2-ligand binding

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Constraining binding hot spots ...... ensation in SH2-ligand binding

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type

label

Constraining binding hot spots ...... ensation in SH2-ligand binding

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Constraining binding hot spots ...... ensation in SH2-ligand binding

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Constraining binding hot spots ...... ensation in SH2-ligand binding

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prefLabel

Constraining binding hot spots ...... ensation in SH2-ligand binding

@ast

Constraining binding hot spots ...... ensation in SH2-ligand binding

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Constraining binding hot spots ...... ensation in SH2-ligand binding

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Journal of the American Chemical Society

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Constraining binding hot spots ...... ensation in SH2-ligand binding

@en

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Carol Beth Post

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

Jianhua Tian

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Joshua M Ward

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Nina M Gorenstein

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Stephen F Martin

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P2860

CHARMM: the biomolecular simulation program

Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors

Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: implications for drug design

Thermodynamic and structural effects of conformational constraints in protein-ligand interactions. Entropic paradoxy associated with ligand preorganization

Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide

Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck

Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode

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11058-11070

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10.1021/JA910535J

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32

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2010-08-01T00:00:00Z

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20698672

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2943377

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