The role of conformational entropy in molecular recognition by calmodulin. - Wikidata - wikimedia - TriplyDB

The role of conformational entropy in molecular recognition by calmodulin.

The role of conformational entropy in molecular recognition by calmodulin.

http://www.wikidata.org/entity/Q34632794

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Correlation as a determinant of configurational entropy in supramolecular and protein systems The ensemble nature of allostery Principles of allosteric interactions in cell signaling Molecular basis of calcium-sensitizing and desensitizing mutations of the human cardiac troponin C regulatory domain: a multi-scale simulation study Conformational frustration in calmodulin-target recognition.Dynamics connect substrate recognition to catalysis in protein kinase A Protein–Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface Area The Structure of the Tiam1 PDZ Domain/ Phospho-Syndecan1 Complex Reveals a Ligand Conformation that Modulates Protein Dynamics Mg 2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active Site Solution Structure and Dynamics of Human Hemoglobin in the Carbonmonoxy Form Mechanistic Insights into the Retaining Glucosyl-3-phosphoglycerate Synthase from Mycobacteria Automated identification of functional dynamic contact networks from X-ray crystallography Keep on moving: discovering and perturbing the conformational dynamics of enzymes On the relationship between NMR-derived amide order parameters and protein backbone entropy changes Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations Conformational Entropy of Intrinsically Disordered Proteins from Amino Acid Triads Long-range intra-protein communication can be transmitted by correlated side-chain fluctuations alone Capturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular Modeling Shortening a loop can increase protein native state entropy.Signaling through dynamic linkers as revealed by PKA The role of slow and fast protein motions in allosteric interactions.Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation.Protein activity regulation by conformational entropy.Banding of NMR-derived methyl order parameters: implications for protein dynamics.Dominant Alcohol-Protein Interaction via Hydration-Enabled Enthalpy-Driven Binding Mechanism Accurate determination of rates from non-uniformly sampled relaxation data.A surprising role for conformational entropy in protein function.Hydrogen tunneling links protein dynamics to enzyme catalysis Importance of protein dynamics during enzymatic C-H bond cleavage catalysis.(19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus.Distinguishing unfolding and functional conformational transitions of calmodulin using ultraviolet resonance Raman spectroscopy.Structural diversity in integrin/talin interactions.Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity.Dynamic multidrug recognition by multidrug transcriptional repressor LmrR.Labeling proteins with fluorophore/thioamide Förster resonant energy transfer pairs by combining unnatural amino acid mutagenesis and native chemical ligation Human germline antibody gene segments encode polyspecific antibodies.An introduction to NMR-based approaches for measuring protein dynamics.The binding mechanisms of intrinsically disordered proteins.Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions.S100 proteins in cancer.

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P2860

The role of conformational entropy in molecular recognition by calmodulin.

http://www.wikidata.org/entity/Q34632794

description

2010 nî lūn-bûn

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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2010 թվականի ապրիլին 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

The role of conformational entropy in molecular recognition by calmodulin.

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The role of conformational entropy in molecular recognition by calmodulin.

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The role of conformational entropy in molecular recognition by calmodulin.

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type

label

The role of conformational entropy in molecular recognition by calmodulin.

@ast

The role of conformational entropy in molecular recognition by calmodulin.

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The role of conformational entropy in molecular recognition by calmodulin.

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prefLabel

The role of conformational entropy in molecular recognition by calmodulin.

@ast

The role of conformational entropy in molecular recognition by calmodulin.

@en

The role of conformational entropy in molecular recognition by calmodulin.

@nl

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Nature Chemical Biology

P1476

The role of conformational entropy in molecular recognition by calmodulin.

@en

P2093

A Joshua Wand

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

Jakob Dogan

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

Kathleen G Valentine

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

Kendra K Frederick

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Michael S Marlow

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P2860

A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase

Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: studies of the kinase activation mechanism

Structural basis for endothelial nitric oxide synthase binding to calmodulin

The CCP4 suite: programs for protein crystallography

Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects

A hot spot of binding energy in a hormone-receptor interface

Coupling of folding and binding for unstructured proteins

Optimal isotope labelling for NMR protein structure determinations.

Insights into the local residual entropy of proteins provided by NMR relaxation.

Temperature dependence of the internal dynamics of a calmodulin-peptide complex.

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10.1038/NCHEMBIO.347

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5

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6

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43100119

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20383153

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3050676

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