Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.
about
Titin-based tension in the cardiac sarcomere: molecular origin and physiological adaptationsForce dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.Mechanical network in titin immunoglobulin from force distribution analysisIsopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenesProtein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative foldingMolecular basis for the structural stability of an enclosed β-barrel loop.Unfolding times for proteins in a force clamp.Photothermal cantilever actuation for fast single-molecule force spectroscopy.A Simple and Practical Spreadsheet-Based Method to Extract Single-Molecule Dissociation Kinetics from Variable Loading-Rate Force Spectroscopy Data.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.Unfolding proteins with an atomic force microscope: force-fluctuation-induced nonexponential kinetics.Single molecule force spectroscopy using polyproteins.Contrasting the individual reactive pathways in protein unfolding and disulfide bond reduction observed within a single protein.Minimum energy compact structures in force-quench polyubiquitin folding are domain swappedDirect quantification of the attempt frequency determining the mechanical unfolding of ubiquitin proteinOptimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments.Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors.Spontaneous dimerization of titin protein Z1Z2 domains induces strong nanomechanical anchoring.The Nanomechanics of Lipid Multibilayer Stacks Exhibits Complex Dynamics.Force-clamp analysis techniques give highest rank to stretched exponential unfolding kinetics in ubiquitin.Solvent molecules bridge the mechanical unfolding transition state of a protein.Mechanical biochemistry of proteins one molecule at a time.Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis.Osmolyte-induced separation of the mechanical folding phases of ubiquitin.Direct observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin.Mechanical characterization of protein L in the low-force regime by electromagnetic tweezers/evanescent nanometry.Single homopolypeptide chains collapse into mechanically rigid conformations.Mechanical unfolding of two DIS RNA kissing complexes from HIV-1.Nanomechanics of HaloTag tethers.Understanding biology by stretching proteins: recent progress.Protein folding under mechanical forces: a physiological view.Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.A conditional gating mechanism assures the integrity of the molecular force-sensor titin kinase.Direct observation of disulfide isomerization in a single protein.Non-exponential kinetics of unfolding under a constant force.Direct observation of markovian behavior of the mechanical unfolding of individual proteins.
P2860
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P2860
Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@en
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@nl
type
label
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@en
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@nl
prefLabel
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@en
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@nl
P2093
P2860
P1433
P1476
Force-clamp spectroscopy of si ...... pathways of I27 and ubiquitin.
@en
P2093
Carmen L Badilla
Jasna Brujić
Julio M Fernández
Sergi Garcia-Manyes
P2860
P304
P356
10.1529/BIOPHYSJ.107.104422
P407
P577
2007-06-01T00:00:00Z