Direct observation of the three-state folding of a single protein molecule.
about
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyMechanical unzipping and rezipping of a single SNARE complex reveals hysteresis as a force-generating mechanismPeroxidase activity and structural transitions of cytochrome c bound to cardiolipin-containing membranesSingle-molecule force spectroscopy distinguishes target binding modes of calmodulinProtein folding: then and nowRatcheting up protein translocation with anthrax toxinThe High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease HStructure, Stability, and Folding of Ribonuclease H1 from the Moderately Thermophilic Chlorobium tepidum : Comparison with Thermophilic and Mesophilic HomologuesWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesChoosing an effective protein bioconjugation strategyThe protein folding problemDirect observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Folding energy landscape and network dynamics of small globular proteinsAnisotropic deformation response of single protein molecules.Protein folding and misfolding: mechanism and principles.Nucleotides regulate the mechanical hierarchy between subdomains of the nucleotide binding domain of the Hsp70 chaperone DnaK.Deconvolution of dynamic mechanical networksProtein folding at single-molecule resolution.Cellular heterogeneity and live cell arrays.Adhesion through single peptide aptamers.High-resolution optical tweezers for single-molecule manipulation.Single-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.Force unfolding kinetics of RNA using optical tweezers. II. Modeling experiments.Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.Single-molecule analysis reveals three phases of DNA degradation by an exonuclease.High-resolution, single-molecule measurements of biomolecular motion.Optical trapping with high forces reveals unexpected behaviors of prion fibrils.Stretching to understand proteins - a survey of the protein data bank.Mechanical unfolding of RNA: from hairpins to structures with internal multiloops.Using optical tweezers for measuring the interaction forces between human bone cells and implant surfaces: System design and force calibration.Theory, analysis, and interpretation of single-molecule force spectroscopy experiments.Ligand-dependent equilibrium fluctuations of single calmodulin molecules.Coexistence of an ILPR i-motif and a partially folded structure with comparable mechanical stability revealed at the single-molecule level.Full distance-resolved folding energy landscape of one single protein molecule.Protein folding and unfolding under forceUnfolding 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.Three powerful research tools from single cells into single molecules: AFM, laser tweezers, and Raman spectroscopy.Free-energy inference from partial work measurements in small systems.
P2860
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P2860
Direct observation of the three-state folding of a single protein molecule.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Direct observation of the three-state folding of a single protein molecule.
@ast
Direct observation of the three-state folding of a single protein molecule.
@en
Direct observation of the three-state folding of a single protein molecule.
@nl
type
label
Direct observation of the three-state folding of a single protein molecule.
@ast
Direct observation of the three-state folding of a single protein molecule.
@en
Direct observation of the three-state folding of a single protein molecule.
@nl
prefLabel
Direct observation of the three-state folding of a single protein molecule.
@ast
Direct observation of the three-state folding of a single protein molecule.
@en
Direct observation of the three-state folding of a single protein molecule.
@nl
P50
P356
P1433
P1476
Direct observation of the three-state folding of a single protein molecule.
@en
P2093
Susan Marqusee
P304
P356
10.1126/SCIENCE.1116702
P407
P577
2005-09-01T00:00:00Z