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The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.

The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.

http://www.wikidata.org/entity/Q33850735

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A flash in the pan: dissecting dynamic amyloid intermediates using fluorescence When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches Investigation of intramolecular dynamics and conformations of α-, β- and γ-synuclein Systematic evaluation of fluorescence correlation spectroscopy data analysis on the nanosecond time scale.The initial step of DNA hairpin folding: a kinetic analysis using fluorescence correlation spectroscopy.Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix.Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: investigation at single molecular resolution.Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions.Fluorescence correlation spectroscopy: past, present, future.The dual-color photon counting histogram with non-ideal photodetectors.Fluorescence quenching by TEMPO: a sub-30 A single-molecule ruler Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.Light chain-dependent self-association of dynein intermediate chain.Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments.A two-dimensional view of the folding energy landscape of cytochrome c Coil-globule transition in the denatured state of a small protein Domain orientation in the N-Terminal PDZ tandem from PSD-95 is maintained in the full-length protein Detecting intramolecular conformational dynamics of single molecules in short distance range with subnanometer sensitivity.A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures.Ultrafast dynamics of protein collapse from single-molecule photon statistics.Dynamics of equilibrium structural fluctuations of apomyoglobin measured by fluorescence correlation spectroscopy.Fluorescence correlation spectroscopic study of serpin depolymerization by computationally designed peptides.Förster resonance energy transfer and protein-induced fluorescence enhancement as synergetic multi-scale molecular rulers Single-molecule biophysics: at the interface of biology, physics and chemistry Single-molecule fluorescence studies of protein folding and conformational dynamics Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa.Fluorescence correlation spectroscopy of finite-sized particles.Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ Barrierless evolution of structure during the submillisecond refolding reaction of a small protein.Protein aggregation processes: In search of the mechanism.Fluorescence characterization of denatured proteins.Collapse transition in proteins Photophysical processes in single molecule organic fluorescent probes.Studies of protein folding and dynamics using single molecule fluorescence spectroscopy.The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.Interconnection of salt-induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution.Managing free-energy barriers in nuclear pore transport.A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties.Direct observation of T4 lysozyme hinge-bending motion by fluorescence correlation spectroscopy.

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P2860

The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.

http://www.wikidata.org/entity/Q33850735

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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The kinetics of conformational ...... sured by fluorescence methods.

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

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The kinetics of conformational ...... sured by fluorescence methods.

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Carl Frieden

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Elliot L Elson

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Krishnananda Chattopadhyay

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P2860

Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate

From Levinthal to pathways to funnels

Measuring dynamic flexibility of the coil state of a helix-forming peptide.

Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.

Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.

Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy.

The protein folding 'speed limit'.

Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy.

Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins.

Measuring the rate of intramolecular contact formation in polypeptides.

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