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Association kinetics from single molecule force spectroscopy measurements.

Association kinetics from single molecule force spectroscopy measurements.

http://www.wikidata.org/entity/Q37282334

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Improved approximations for some polymer extension models A Rough Energy Landscape to Describe Surface-Linked Antibody and Antigen Bond Formation.A flexible nanoarray approach for the assembly and probing of molecular complexes.Kinetics of the multistep rupture of fibrin 'A-a' polymerization interactions measured using atomic force microscopy Hidden multiple bond effects in dynamic force spectroscopy.Analysis of affinities between specific biological ligands using atomic force microscopy.Atomic force microscopy-based molecular studies on the recognition of immunogenic chlorinated ovalbumin by macrophage receptors.Single Molecule Force Spectroscopy to Compare Natural versus Artificial Antibody-Antigen Interaction.

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P2860

Association kinetics from single molecule force spectroscopy measurements.

http://www.wikidata.org/entity/Q37282334

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on April 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Association kinetics from single molecule force spectroscopy measurements.

@en

Association kinetics from single molecule force spectroscopy measurements.

@nl

type

label

Association kinetics from single molecule force spectroscopy measurements.

@en

Association kinetics from single molecule force spectroscopy measurements.

@nl

prefLabel

Association kinetics from single molecule force spectroscopy measurements.

@en

Association kinetics from single molecule force spectroscopy measurements.

@nl

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J.BPJ.2009.01.031

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Biophysical Journal

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Association kinetics from single molecule force spectroscopy measurements.

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Boris B Akhremitchev

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Chad Ray

http://www.w3.org/2001/XMLSchema#string

Nimit Lad

http://www.w3.org/2001/XMLSchema#string

Senli Guo

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P2860

Single molecule force spectroscopy in biology using the atomic force microscope.

Molecular recognition imaging and force spectroscopy of single biomolecules.

Strength of multiple parallel biological bonds

Pairwise interactions between linear alkanes in water measured by AFM force spectroscopy.

Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.

Streptavidin-biotin binding energetics.

Dynamic strength of molecular adhesion bonds

Molecular dynamics study of unbinding of the avidin-biotin complex.

Reduction-of-dimensionality kinetics at reaction-limited cell surface receptors

Force spectroscopy of the double-tethered concanavalin-A mannose bond.

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3412-3422

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scholarly article

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10.1016/J.BPJ.2009.01.031

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