Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches.
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What determines the strength of noncovalent association of ligands to proteins in aqueous solution?The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding siteThe maximal affinity of ligandsComputational approaches in target identification and drug discoveryRational approaches to improving selectivity in drug designA structural snapshot of an intermediate on the streptavidin-biotin dissociation pathwayStructure and dynamics of thioguanine-modified duplex DNAHow the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramerAbsolute free energy of binding of avidin/biotin, revisitedCalculation of the Absolute Free Energy of Binding and Related Entropies with the HSMD-TI Method: The FKBP12-L8 ComplexInsight on Mutation-Induced Resistance from Molecular Dynamics Simulations of the Native and Mutated CSF-1R and KITFunctional loop dynamics of the streptavidin-biotin complexToward detection of DNA-bound proteins using solid-state nanopores: insights from computer simulations.Molecular dynamics study of unbinding of the avidin-biotin complex.The statistical-thermodynamic basis for computation of binding affinities: a critical reviewThe relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.On the calculation of absolute macromolecular binding free energiesFree energy decomposition of protein-protein interactions.Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidinComputational carbohydrate chemistry: what theoretical methods can tell usAssessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations.Activation of the edema factor of Bacillus anthracis by calmodulin: evidence of an interplay between the EF-calmodulin interaction and calcium binding.Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120The Carboxy Terminus of the Ligand Peptide Determines the Stability of the MHC Class I Molecule H-2Kb: A Combined Molecular Dynamics and Experimental Study.Recent theoretical and computational advances for modeling protein-ligand binding affinitiesProtein-protein recognition: an experimental and computational study of the R89K mutation in Raf and its effect on Ras bindingSeparated topologies--a method for relative binding free energy calculations using orientational restraints.A streptavidin mutant with altered ligand-binding specificityThe origin of the cooperativity in the streptavidin-biotin system: A computational investigation through molecular dynamics simulations.Directed evolution of streptavidin variants using in vitro compartmentalization.Diagnostic devices as biomaterials: a review of nucleic acid and protein microarray surface performance issues.Force field bias in protein folding simulationsMethods for calculating the entropy and free energy and their application to problems involving protein flexibility and ligand binding.Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel.Leucine 18, a hydrophobic residue essential for high affinity binding of anthopleurin B to the voltage-sensitive sodium channel.Strictly conserved lysine of prolyl-tRNA Synthetase editing domain facilitates binding and positioning of misacylated tRNA(Pro.).Methods for calculating the absolute entropy and free energy of biological systems based on ideas from polymer physics.Free energy calculations and molecular dynamics simulations of wild-type and variants of the DNA-EcoRI complex.Contribution of translational and rotational motions to molecular association in aqueous solution.Fundamentals of drug design from a biophysical viewpoint.
P2860
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P2860
Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh-hant
name
Absolute and relative binding ...... nergy perturbation approaches.
@en
Absolute and relative binding ...... nergy perturbation approaches.
@nl
type
label
Absolute and relative binding ...... nergy perturbation approaches.
@en
Absolute and relative binding ...... nergy perturbation approaches.
@nl
prefLabel
Absolute and relative binding ...... nergy perturbation approaches.
@en
Absolute and relative binding ...... nergy perturbation approaches.
@nl
P356
P1433
P1476
Absolute and relative binding ...... nergy perturbation approaches.
@en
P2093
Kollman PA
Miyamoto S
P2860
P304
P356
10.1002/PROT.340160303
P407
P577
1993-07-01T00:00:00Z