The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
about
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyForce dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative foldingMolecular basis for the structural stability of an enclosed β-barrel loop.Exploring the energy landscape of GFP by single-molecule mechanical experiments.The mechanical unfolding of ubiquitin through all-atom Monte Carlo simulation with a Go-type potential.Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.On the remarkable mechanostability of scaffoldins and the mechanical clamp motif.S-glutathionylation of cryptic cysteines enhances titin elasticity by blocking protein folding.Reversible mechanical unfolding of single ubiquitin molecules.Simultaneous atomic force microscope and fluorescence measurements of protein unfolding using a calibrated evanescent wave.Effect of ion-binding and chemical phospholipid structure on the nanomechanics of lipid bilayers studied by force spectroscopy.Sub-angstrom conformational changes of a single molecule captured by AFM variance analysis.Breaking bonds in the atomic force microscope: theory and analysis.Quasi-simultaneous imaging/pulling analysis of single polyprotein molecules by atomic force microscopy.Dynamics of single-molecule force-ramp experiments: The role of fluctuations.Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.Theory, analysis, and interpretation of single-molecule force spectroscopy experiments.Discovery through the computational microscope.A Simple and Practical Spreadsheet-Based Method to Extract Single-Molecule Dissociation Kinetics from Variable Loading-Rate Force Spectroscopy Data.Sampling protein form and function with the atomic force microscope.Mechanical forces regulate the reactivity of a thioester bond in a bacterial adhesinFusion of biomimetic stealth probes into lipid bilayer coresUnfolding the A2 domain of von Willebrand factor with the optical trapMechanically unfolding protein L using a laser-feedback-controlled cantilever.Collapse dynamics of single proteins extended by force.Single-molecule force spectroscopy approach to enzyme catalysis.Probing osmolyte participation in the unfolding transition state of a protein.Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy.Role of conservative mutations in protein multi-property adaptationDissecting the mechanical unfolding of ubiquitin.Unfolding proteins with an atomic force microscope: force-fluctuation-induced nonexponential kinetics.The complex folding network of single calmodulin molecules.Protein high-force pulling simulations yield low-force results.Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1Single molecule force spectroscopy using polyproteins.Temperature sculpting in yoctoliter volumes.Probing the mechanical folding kinetics of TAR RNA by hopping, force-jump, and force-ramp methods.Mechanical resistance of proteins explained using simple molecular modelsAtomic force microscope based biomolecular force-clamp measurements using a micromachined electrostatic actuator.
P2860
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P2860
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@ast
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@en
type
label
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@ast
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@en
prefLabel
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@ast
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@en
P2093
P2860
P356
P1476
The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
@en
P2093
Hongbin Li
Julio M Fernandez
Michael Schlierf
P2860
P304
P356
10.1073/PNAS.0400033101
P407
P577
2004-04-27T00:00:00Z