The F130L mutation in streptavidin reduces its binding affinity to biotin through electronic polarization effect.
about
Structural and physico-chemical effects of disease and non-disease nsSNPs on proteinsFunctional loop dynamics of the streptavidin-biotin complexProbing Origin of Binding Difference of inhibitors to MDM2 and MDMX by Polarizable Molecular Dynamics Simulation and QM/MM-GBSA CalculationThe origin of the cooperativity in the streptavidin-biotin system: A computational investigation through molecular dynamics simulations.Large-scale molecular dynamics simulation: Effect of polarization on thrombin-ligand binding energyThermodynamics calculation of protein-ligand interactions by QM/MM polarizable charge parameters.Improving the Solubility of Artificial Ligands of Streptavidin to Enable More Practical Reversible Switching of Protein Localization in Cells.Accessing the applicability of polarized protein-specific charge in linear interaction energy analysis.
P2860
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P2860
The F130L mutation in streptavidin reduces its binding affinity to biotin through electronic polarization effect.
description
2013 nî lūn-bûn
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2013年の論文
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name
The F130L mutation in streptav ...... lectronic polarization effect.
@en
The F130L mutation in streptav ...... lectronic polarization effect.
@nl
type
label
The F130L mutation in streptav ...... lectronic polarization effect.
@en
The F130L mutation in streptav ...... lectronic polarization effect.
@nl
prefLabel
The F130L mutation in streptav ...... lectronic polarization effect.
@en
The F130L mutation in streptav ...... lectronic polarization effect.
@nl
P2860
P50
P356
P1476
The F130L mutation in streptav ...... electronic polarization effect
@en
P2093
P2860
P304
P356
10.1002/JCC.23421
P577
2013-09-02T00:00:00Z