Cooperative hydrogen bond interactions in the streptavidin-biotin system - Wikidata - awgldk - TriplyDB

Cooperative hydrogen bond interactions in the streptavidin-biotin system

Cooperative hydrogen bond interactions in the streptavidin-biotin system

http://www.wikidata.org/entity/Q36473994

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The origins of femtomolar protein-ligand binding: hydrogen-bond cooperativity and desolvation energetics in the biotin-(strept)avidin binding site Superglue from bacteria: unbreakable bridges for protein nanotechnology Tamavidins--novel avidin-like biotin-binding proteins from the Tamogitake mushroom Structural and functional characteristics of xenavidin, the first frog avidin from Xenopus tropicalis A Distal Point Mutation in the Streptavidin−Biotin Complex Preserves Structure but Diminishes Binding Affinity: Experimental Evidence of Electronic Polarization Effects?How the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramer Evolved streptavidin mutants reveal key role of loop residue in high-affinity binding Streptavidin and its biotin complex at atomic resolution The structure of the SBP-Tag-streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits.Contamination from an affinity column: an encounter with a new villain in the world of membrane-protein crystallization Functional loop dynamics of the streptavidin-biotin complex Single-molecule detection of a guanine(C8) - thymine(N3) cross-link using ion channel recording Toward detection of DNA-bound proteins using solid-state nanopores: insights from computer simulations.Combinatorial methods for small-molecule placement in computational enzyme design.Staggered Mesh Ewald: An extension of the Smooth Particle-Mesh Ewald method adding great versatility.Comparison of binding platforms yields insights into receptor binding differences between shiga toxins 1 and 2 Titanium-silicon oxide film structures for polarization-modulated infrared reflection absorption spectroscopy Rates and equilibria for probe capture by an antibody with infinite affinity.Construction of chimeric dual-chain avidin by tandem fusion of the related avidins.Label-free microcavity biosensors: steps towards personalized medicine.Motifs for molecular recognition exploiting hydrophobic enclosure in protein-ligand binding 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.Simulations of a protein crystal: explicit treatment of crystallization conditions links theory and experiment in the streptavidin-biotin complex.Dynamics of the streptavidin-biotin complex in solution and in its crystal lattice: distinct behavior revealed by molecular simulations.Pulsed IR heating studies of single-molecule DNA duplex dissociation kinetics and thermodynamics.Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration.Salt bridge exchange binding mechanism between streptavidin and its DNA aptamer--thermodynamics and spectroscopic evidences.The drug-target residence time model: a 10-year retrospective.Regulation of integrin adhesions by varying the density of substrate-bound epidermal growth factor.Transtactin: a universal transmembrane delivery system for Strep-tag II-fused cargos.Rationalizing tight ligand binding through cooperative interaction networks.A Streptavidin Binding Site Mutation Yields an Unexpected Result: An Ionized Asp128 Residue Is Not Essential for Strong Biotin Binding.Thermodynamics calculation of protein-ligand interactions by QM/MM polarizable charge parameters.The cryo-EM structure of the UPF-EJC complex shows UPF1 poised toward the RNA 3' end.Control of enzyme reactions by a reconfigurable DNA nanovault.Electrical Current Signatures of DNA Base Modifications in Single Molecules Immobilized in the α-Hemolysin Ion Channel.Cys-Cys cross-linking shows contact between the N-terminus of lethal factor and Phe427 of the anthrax toxin pore Single and multiple bonds in (strept)avidin-biotin interactions.The F130L mutation in streptavidin reduces its binding affinity to biotin through electronic polarization effect.

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P2860

Cooperative hydrogen bond interactions in the streptavidin-biotin system

http://www.wikidata.org/entity/Q36473994

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2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年學術文章

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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Protein Science

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Cooperative hydrogen bond interactions in the streptavidin-biotin system

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David E Hyre

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Ethan A Merritt

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Isolde Le Trong

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John F Eccleston

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N Michael Green

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Patrick S Stayton

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Ronald E Stenkamp

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P2860

Crystal structure of core streptavidin determined from multiwavelength anomalous diffraction of synchrotron radiation

A structural snapshot of an intermediate on the streptavidin-biotin dissociation pathway

Ser45 plays an important role in managing both the equilibrium and transition state energetics of the streptavidin-biotin system

Structural origins of high-affinity biotin binding to streptavidin

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

SHELXL: high-resolution refinement

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase

Second-order kinetic analysis of IAsys biosensor data: its use and applicability.

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10.1110/PS.051970306

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3

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15

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16452627

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2249767

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