Limiting assumptions in structure-based design: binding entropy. - Wikidata - awgldk - TriplyDB

Limiting assumptions in structure-based design: binding entropy.

Limiting assumptions in structure-based design: binding entropy.

http://www.wikidata.org/entity/Q37972732

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Beyond Membrane Protein Structure: Drug Discovery, Dynamics and Difficulties.A structure-based design of new C2- and C13-substituted taxanes: tubulin binding affinities and extended quantitative structure-activity relationships using comparative binding energy (COMBINE) analysis.New in silico and conventional in vitro approaches to advance HIV drug discovery and design.Current progress in Structure-Based Rational Drug Design marks a new mindset in drug discovery Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis.Microscopic insights into the NMR relaxation-based protein conformational entropy meter Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.Limiting assumptions in molecular modeling: electrostatics.Helix stability of oligoglycine, oligoalanine, and oligo-β-alanine dodecamers reflected by hydrogen-bond persistence.

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P2860

Limiting assumptions in structure-based design: binding entropy.

http://www.wikidata.org/entity/Q37972732

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article científic

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article scientifique

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artigo científico

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artikel ilmiah

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artículo científico

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Limiting assumptions in structure-based design: binding entropy.

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Limiting assumptions in structure-based design: binding entropy.

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type

label

Limiting assumptions in structure-based design: binding entropy.

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Limiting assumptions in structure-based design: binding entropy.

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prefLabel

Limiting assumptions in structure-based design: binding entropy.

@en

Limiting assumptions in structure-based design: binding entropy.

@nl

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Journal of Computer - Aided Molecular Design

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Limiting assumptions in structure-based design: binding entropy.

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Garland R Marshall

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P2860

Intrinsically Disordered Proteins in Human Diseases: Introducing the D 2 Concept

Long distance PELDOR measurements on the histone core particle

Structural and energetic aspects of Grb2-SH2 domain-swapping

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

Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.

Direct conversion of EPR dipolar time evolution data to distance distributions.

Solution structure of HIV-1 protease flaps probed by comparison of molecular dynamics simulation ensembles and EPR experiments.

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

Binding of flexible and constrained ligands to the Grb2 SH2 domain: structural effects of ligand preorganization.

Distance measurements in the nanometer range by pulse EPR.

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s10822-011-9494-1

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