Contributions to the binding free energy of ligands to avidin and streptavidin. - Wikidata - awgldk - TriplyDB

Contributions to the binding free energy of ligands to avidin and streptavidin.

Contributions to the binding free energy of ligands to avidin and streptavidin.

http://www.wikidata.org/entity/Q43947466

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The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site 3'-axial CH2 OH substitution on glucopyranose does not increase glycogen phosphorylase inhibitory potency. QM/MM-PBSA calculations suggest why Structure-based engineering of streptavidin monomer with a reduced biotin dissociation rate Theory of free energy and entropy in noncovalent binding Absolute free energy of binding of avidin/biotin, revisited Efficient Computation of Small-Molecule Configurational Binding Entropy and Free Energy Changes by Ensemble Enumeration Structural and dynamic determinants of protein-peptide recognition.Alchemical free energy methods for drug discovery: progress and challenges Structural and energetic analysis of 2-aminobenzimidazole inhibitors in complex with the hepatitis C virus IRES RNA using molecular dynamics simulations.A new method to estimate ligand-receptor energetics.Flexibility of a biotinylated ligand in artificial metalloenzymes based on streptavidin--an insight from molecular dynamics simulations with classical and ab initio force fields.Large scale affinity calculations of cyclodextrin host-guest complexes: Understanding the role of reorganization in the molecular recognition process.Identification of aldehyde dehydrogenase 1A1 modulators using virtual screening.Formation pathways of a guanine-quadruplex DNA revealed by molecular dynamics and thermodynamic analysis of the substates.Revisiting free energy calculations: a theoretical connection to MM/PBSA and direct calculation of the association free energy A comprehensive examination of the contributions to the binding entropy of protein-ligand complexes.Calculating the free energy of association of transmembrane helices Absolute binding free energy calculations using molecular dynamics simulations with restraining potentials.Ligand configurational entropy and protein binding.Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding Recognition of ribonuclease A by 3'-5'-pyrophosphate-linked dinucleotide inhibitors: a molecular dynamics/continuum electrostatics analysis.New insights into Vitamin D sterol-VDR proteolysis, allostery, structure-function from the perspective of a conformational ensemble model.Molecular dynamics in drug design: new generations of compstatin analogs.Modeling fatty acid delivery from intestinal fatty acid binding protein to a membrane Molecular dynamics: survey of methods for simulating the activity of proteins.Binding efficiency of protein-protein complexes.Electrostatic properties of cowpea chlorotic mottle virus and cucumber mosaic virus capsids Molecular mechanisms and design principles for promiscuous inhibitors to avoid drug resistance: lessons learned from HIV-1 protease inhibition.Binding of small-molecule ligands to proteins: "what you see" is not always "what you get".Salt bridge exchange binding mechanism between streptavidin and its DNA aptamer--thermodynamics and spectroscopic evidences.Kinetics, in silico docking, molecular dynamics, and MM-GBSA binding studies on prototype indirubins, KT5720, and staurosporine as phosphorylase kinase ATP-binding site inhibitors: the role of water molecules examined.Insight into G-DNA structural polymorphism and folding from sequence and loop connectivity through free energy analysis.Disulfide-mediated stabilization of the IκB kinase binding domain of NF-κB essential modulator (NEMO).Hydration Site Thermodynamics Explain SARs for Triazolylpurines Analogues Binding to the A2A Receptor Aptahistochemistry in diagnostic pathology: technical scrutiny and feasibility.In Silico Prediction of Interactions between Site II on Human Serum Albumin and Profen Drugs.New method for calculating the absolute free energy of binding: the effect of a mobile loop on the avidin/biotin complex Calculation of absolute protein-ligand binding affinity using path and endpoint approaches.Relative stability of the open and closed conformations of the active site loop of streptavidin Elucidating the energetics of entropically driven protein-ligand association: calculations of absolute binding free energy and entropy.

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P2860

Contributions to the binding free energy of ligands to avidin and streptavidin.

http://www.wikidata.org/entity/Q43947466

description

2002 nî lūn-bûn

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2002年學術文章

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name

Contributions to the binding free energy of ligands to avidin and streptavidin.

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Contributions to the binding free energy of ligands to avidin and streptavidin.

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type

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Contributions to the binding free energy of ligands to avidin and streptavidin.

@en

Contributions to the binding free energy of ligands to avidin and streptavidin.

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prefLabel

Contributions to the binding free energy of ligands to avidin and streptavidin.

@en

Contributions to the binding free energy of ligands to avidin and streptavidin.

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Contributions to the binding free energy of ligands to avidin and streptavidin

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Francois Gandolfo

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Themis Lazaridis

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P2860

What determines the strength of noncovalent association of ligands to proteins in aqueous solution?

The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core

Crystal structure and ligand-binding studies of a screened peptide complexed with streptavidin

Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate

Structural origins of high-affinity biotin binding to streptavidin

Binding to protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence

Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 A resolution

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

Effective energy function for proteins in solution

Discrimination of the native from misfolded protein models with an energy function including implicit solvation

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10.1002/PROT.10086

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