Theoretical analysis of single-molecule force spectroscopy experiments: heterogeneity of chemical bonds.
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Refined procedure of evaluating experimental single-molecule force spectroscopy data.Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.Force-induced lysozyme--HyHEL5 antibody dissociation and its analysis by means of a cooperative binding model.Unfolding proteins with an atomic force microscope: force-fluctuation-induced nonexponential kinetics.Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactionsAntibody-unfolding and metastable-state binding in force spectroscopy and recognition imagingLong lifetime of hydrogen-bonded DNA basepairs by force spectroscopy.A structural, kinetic model of soft tissue thermomechanics.Directly measuring single-molecule heterogeneity using force spectroscopy.Quantitative analysis of single-molecule RNA-protein interaction.Analysis of DNA interactions using single-molecule force spectroscopy.Quantitative analysis of the nanopore translocation dynamics of simple structured polynucleotides.Two barriers or not? Dynamic force spectroscopy on the integrin α7β1 invasin complex.Mechanical stability of bivalent transition metal complexes analyzed by single-molecule force spectroscopy.Hidden multiple bond effects in dynamic force spectroscopy.Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions.Statistics of forced thermally activated escape events out of a metastable state: most probable escape force and escape-force moments.Size-Dependent Affinity of Glycine and Its Short Oligomers to Pyrite Surface: A Model for Prebiotic Accumulation of Amino Acid Oligomers on a Mineral Surface.Manipulating and probing enzymatic conformational fluctuations and enzyme-substrate interactions by single-molecule FRET-magnetic tweezers microscopy.Exploring hysteresis and energy dissipation in single-molecule force spectroscopy.Observing the osmophobic effect in action at the single molecule levelMaximum likelihood estimation of protein kinetic parameters under weak assumptions from unfolding force spectroscopy experimentsStatistics of reversible bond dynamics observed in force-clamp spectroscopyDynamic force spectroscopy: Analysis of reversible bond-breaking dynamics
P2860
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P2860
Theoretical analysis of single-molecule force spectroscopy experiments: heterogeneity of chemical bonds.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Theoretical analysis of single ...... terogeneity of chemical bonds.
@en
type
label
Theoretical analysis of single ...... terogeneity of chemical bonds.
@en
prefLabel
Theoretical analysis of single ...... terogeneity of chemical bonds.
@en
P2093
P2860
P1433
P1476
Theoretical analysis of single ...... eterogeneity of chemical bonds
@en
P2093
F W Bartels
M Evstigneev
M Nguyen-Duong
P2860
P304
P356
10.1529/BIOPHYSJ.105.077099
P407
P577
2006-03-02T00:00:00Z