Fluorescence quenching: A tool for single-molecule protein-folding study. - Wikidata - wikimedia - TriplyDB

Fluorescence quenching: A tool for single-molecule protein-folding study.

Fluorescence quenching: A tool for single-molecule protein-folding study.

http://www.wikidata.org/entity/Q35839147

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Mineral and Protein-Bound Water and Latching Action Control Mechanical Behavior at Protein-Mineral Interfaces in Biological Nanocomposites Force-induced unfolding of fibronectin in the extracellular matrix of living cells tRNA binding to antitumor drug doxorubicin and its analogue Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion.Ultrasound-modulated fluorescence based on donor-acceptor-labeled microbubbles.Ultrasound-modulated fluorescence based on fluorescent microbubbles Systematic evaluation of fluorescence correlation spectroscopy data analysis on the nanosecond time scale.Thermodynamic and kinetic aspects of RNA pulling experiments.Fluorescence-tracking of activation gating in human ERG channels reveals rapid S4 movement and slow pore opening Single-molecule studies of the neuronal SNARE fusion machinery.The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.Global configuration of single titin molecules observed through chain-associated rhodamine dimers Probing conformational changes of gramicidin ion channels by single-molecule patch-clamp fluorescence microscopy.Nanochannel-based single molecule recycling.Fluorescence quenching by TEMPO: a sub-30 A single-molecule ruler Codon-dependent tRNA fluctuations monitored with fluorescence polarization.Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.Light chain-dependent self-association of dynein intermediate chain.DNA origami-based standards for quantitative fluorescence microscopy.Fluorescence spectroscopy of single molecules under ambient conditions: methodology and technology.Detecting intramolecular conformational dynamics of single molecules in short distance range with subnanometer sensitivity.Single-molecule studies highlight conformational heterogeneity in the early folding steps of a large ribozyme Dynamics of synaptic SfiI-DNA complex: single-molecule fluorescence analysis.Advances in surface-enhanced fluorescence.Detection of the opening of the bundle crossing in KcsA with fluorescence lifetime spectroscopy reveals the existence of two gates for ion conduction Single-molecule fluorescence studies of protein folding and conformational dynamics Dynamics of green fluorescent protein mutant2 in solution, on spin-coated glasses, and encapsulated in wet silica gels.Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ Type 3 Secretion Translocators Spontaneously Assemble a Hexadecameric Transmembrane Complex A fluorescence based method for the quantification of surface functional groups in closed micro- and nanofluidic channels.Folding and unfolding of chromophoric foldamers show unusual colorful single molecule spectral dynamics.Fluorescence characterization of denatured proteins.Leukocyte proteases cleave von Willebrand factor at or near the ADAMTS13 cleavage site Release of the self-quenching of fluorescence near silver metallic surfaces.Photophysical processes in single molecule organic fluorescent probes.Single-molecule studies of riboswitch folding.Studies of protein folding and dynamics using single molecule fluorescence spectroscopy.A direct, continuous, sensitive assay for protein disulphide-isomerase based on fluorescence self-quenching The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.The citrate carrier CitS probed by single-molecule fluorescence spectroscopy.

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P2860

Fluorescence quenching: A tool for single-molecule protein-folding study.

http://www.wikidata.org/entity/Q35839147

description

2000 nî lūn-bûn

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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2000年论文

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2000年论文

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name

Fluorescence quenching: A tool for single-molecule protein-folding study.

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Fluorescence quenching: A tool for single-molecule protein-folding study.

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Fluorescence quenching: A tool for single-molecule protein-folding study.

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Fluorescence quenching: A tool for single-molecule protein-folding study.

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Fluorescence quenching: A tool for single-molecule protein-folding study.

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Fluorescence quenching: A tool for single-molecule protein-folding study.

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PNAS.97.26.14241

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Fluorescence quenching: A tool for single-molecule protein-folding study.

@en

P2093

H D Kim

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S Chu

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S Labeit

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P2860

Titins: giant proteins in charge of muscle ultrastructure and elasticity

The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains

From Levinthal to pathways to funnels

Theory of protein folding: the energy landscape perspective.

Unfolding pathways of individual bacteriorhodopsins.

Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments

The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line.

I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure

Myofibrils bear most of the resting tension in frog skeletal muscle.

Folding-unfolding transitions in single titin molecules characterized with laser tweezers.

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26

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97

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12207723

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P698

11121030

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P921

protein folding

P932

18902

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