Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. - Wikidata - awgldk - TriplyDB

Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.

Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.

http://www.wikidata.org/entity/Q30478703

about

Photophysics of fluorescent probes for single-molecule biophysics and super-resolution imaging Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment A simple model predicts experimental folding rates and a hub-like topology Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model Better biomolecule thermodynamics from kinetics.Single-molecule FRET of protein structure and dynamics - a primer.UV-CD12: synchrotron radiation circular dichroism beamline at ANKA.Effect of flexibility and cis residues in single-molecule FRET studies of polyproline.Importance of backbone and solvent properties for conformational dynamics in polypeptides.Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.Fast protein folding kinetics Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles (RASP).Collapse dynamics of single proteins extended by force.The origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein folding Extremely slow intramolecular diffusion in unfolded protein L Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Fast single-molecule FRET spectroscopy: theory and experiment Combining MFD and PIE for accurate single-pair Förster resonance energy transfer measurements.Theory of the energy transfer efficiency and fluorescence lifetime distribution in single-molecule FRET Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy Protein folding studied by single-molecule FRET.Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins.Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.The assembly dynamics of the cytolytic pore toxin ClyA.Accounting for dye diffusion and orientation when relating FRET measurements to distances: three simple computational methods.Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations.Extracting intrinsic dynamic parameters of biomolecular folding from single-molecule force spectroscopy experiments.Random coil negative control reproduces the discrepancy between scattering and FRET measurements of denatured protein dimensions.Ultrafast dynamics of protein collapse from single-molecule photon statistics.Quantitative interpretation of FRET experiments via molecular simulation: force field and validation.Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering Signatures of hydrophobic collapse in extended proteins captured with force spectroscopy.Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements.Protein hydrophobic collapse and early folding steps observed in a microfluidic mixer.

P2860

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P2860

Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.

http://www.wikidata.org/entity/Q30478703

description

2006 nî lūn-bûn

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2006年の論文

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Mapping protein collapse with ...... rcular dichroism spectroscopy.

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

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Mapping protein collapse with ...... rcular dichroism spectroscopy.

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P2093

Armin Hoffmann

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Avinash Kane

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Benjamin Schuler

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Daniel Nettels

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David A Horsley

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David E Hertzog

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Olgica Bakajin

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Peter Baumgärtel

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P2860

Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima

A theoretical search for folding/unfolding nuclei in three-dimensional protein structures

A surprising simplicity to protein folding.

Analysis of circular dichroism data.

Data registration and selective single-molecule analysis using multi-parameter fluorescence detection.

Statistical coil model of the unfolded state: resolving the reconciliation problem.

Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins.

Specific collapse followed by slow hydrogen-bond formation of beta-sheet in the folding of single-chain monellin

Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence.

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy.

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105-110

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