Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.
about
Direct Reading of Bona Fide Barcode Assays for Diagnostics with Smartphone AppsQuantitative description of thermodynamic and kinetic properties of the platelet factor 4/heparin bonds.Discovery through the computational microscope.Quantitative modeling assesses the contribution of bond strengthening, rebinding and force sharing to the avidity of biomolecule interactions.Long lifetime of hydrogen-bonded DNA basepairs by force spectroscopy.Adhesion of mussel foot protein Mefp-5 to mica: an underwater superglue.A simple bioconjugate attachment protocol for use in single molecule force spectroscopy experiments based on mixed self-assembled monolayers.Association kinetics from single molecule force spectroscopy measurements.Cytoadherence of erythrocytes invaded by Plasmodium falciparum: quantitative contact-probing of a human malaria receptor.Kinetics of the multistep rupture of fibrin 'A-a' polymerization interactions measured using atomic force microscopyTransition model for ricin-aptamer interactions with multiple pathways and energy barriers.Force measurement enabling precise analysis by dynamic force spectroscopy.Hidden multiple bond effects in dynamic force spectroscopy.Unbinding forces of single pertussis toxin-antibody complexes measured by atomic force spectroscopy correlate with their dissociation rates determined by surface plasmon resonance.Single and multiple bonds in (strept)avidin-biotin interactions.Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions.Analysis of affinities between specific biological ligands using atomic force microscopy.pH-Dependent Deformations of the Energy Landscape of Avidin-like Proteins Investigated by Single Molecule Force Spectroscopy
P2860
Q30656033-79F147AA-69B8-4FD2-8939-77F50E4064E0Q33422889-F45D8798-0561-4214-B42C-40D780A5D187Q33511109-4608D7F2-740C-4645-AFAA-578F48D3CC74Q34424986-93E9D8A3-654E-4C2A-9DD3-F2C93DEFEAE7Q35962529-0BBD9339-A373-4331-9C30-BFE53A9256B2Q36190883-0EF0060E-1358-4677-8115-01740A6A71FCQ36396597-FD1D7083-B2D5-41A9-AB49-B7C4F185EB39Q37282334-77DBBCD5-CF4E-4BEC-9CE2-F82CF3235B35Q37408511-85AD910F-9E37-41E9-924A-D56D9D798AB5Q37418794-55A5AC0B-839F-49AD-ADE2-31D9748316C4Q38303306-F0816544-7766-42F8-A0C5-A3FE3E9CAD1BQ40771502-8A1DB6D6-C456-4433-80F3-DAFCED01477EQ42107933-75D1245A-ECDA-4100-BF8E-E4F4CF5099B4Q43765382-FFAC16FE-0276-4769-9329-2BDA6A72FAE3Q44253993-947A6FC7-94C1-4369-93A4-C64DA1F1C4EAQ44264111-16AF07C1-0BAE-4F74-A84E-364A75781825Q45021541-EBA184ED-F6EB-4A89-AC9E-5F2836B46608Q58459342-48404209-8150-45B3-B9AF-3691CED102F3
P2860
Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@ast
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@en
type
label
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@ast
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@en
prefLabel
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@ast
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@en
P2093
P2860
P1433
P1476
Effects of multiple-bond ruptu ...... tin-streptavidin interactions.
@en
P2093
Andrea Kirkpatrick
P2860
P304
P356
10.1529/BIOPHYSJ.108.133900
P407
P577
2008-07-11T00:00:00Z