about
The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding siteRapid Macrocycle Threading by a Fluorescent Dye-Polymer Conjugate in Water with Nanomolar Affinity.How the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramerStreptavidin and its biotin complex at atomic resolutionDevelopment of a Tetrameric Streptavidin Mutein with Reversible Biotin Binding Capability: Engineering a Mobile Loop as an Exit Door for BiotinPlug-and-Play Pairing via Defined Divalent StreptavidinsStructure-based design of a streptavidin mutant specific for an artificial biotin analogueFunctional loop dynamics of the streptavidin-biotin complexQuantifying the stabilizing effects of protein-ligand interactions in the gas phaseA peptide tag system for facile purification and single-molecule immobilizationAccelerating phage-display library selection by reversible and site-specific biotinylation.Structure-guided design of an engineered streptavidin with reusability to purify streptavidin-binding peptide tagged proteins or biotinylated proteins.A New Versatile Immobilization Tag Based on the Ultra High Affinity and Reversibility of the Calmodulin-Calmodulin Binding Peptide Interaction.Reversible major histocompatibility complex I-peptide multimers containing Ni(2+)-nitrilotriacetic acid peptides and histidine tags improve analysis and sorting of CD8(+) T cellsTandem gramicidin channels cross-linked by streptavidin.The 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.Association kinetics from single molecule force spectroscopy measurements.Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase.Salt bridge exchange binding mechanism between streptavidin and its DNA aptamer--thermodynamics and spectroscopic evidences.Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidinsA Streptavidin Binding Site Mutation Yields an Unexpected Result: An Ionized Asp128 Residue Is Not Essential for Strong Biotin Binding.Label-free plasmonic detection of biomolecular binding by a single gold nanorod.Controlling Multivalent Binding through Surface Chemistry: Model Study on Streptavidin.Direct visualization of ligand-protein interactions using atomic force microscopy.Dissociation kinetics of the streptavidin-biotin interaction measured using direct electrospray ionization mass spectrometry analysis.The role of polymer spacers in specific adhesion.Single Pair Förster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Streptavidin-biotin binding energetics.
@ast
Streptavidin-biotin binding energetics.
@en
type
label
Streptavidin-biotin binding energetics.
@ast
Streptavidin-biotin binding energetics.
@en
prefLabel
Streptavidin-biotin binding energetics.
@ast
Streptavidin-biotin binding energetics.
@en
P2093
P1433
P1476
Streptavidin-biotin binding energetics.
@en
P2093
Chilkoti A
Le Trong I
Lybrand TP
Penzotti JE
Stayton PS
Stenkamp RE
P356
10.1016/S1050-3862(99)00042-X
P577
1999-12-01T00:00:00Z