Measuring the rate of intramolecular contact formation in polypeptides. - Test2 - elhamkhani - TriplyDB

Measuring the rate of intramolecular contact formation in polypeptides.

Measuring the rate of intramolecular contact formation in polypeptides.

http://www.wikidata.org/entity/Q35155346

about

Unfolded-state dynamics and structure of protein L characterized by simulation and experiment When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches Investigation of intramolecular dynamics and conformations of α-, β- and γ-synuclein Effects of Mutations on the Reconfiguration Rate of α-Synuclein Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain.The effects of nonnative interactions on protein folding rates: theory and simulation Systematic evaluation of fluorescence correlation spectroscopy data analysis on the nanosecond time scale.Cytochrome c' folding triggered by electron transfer: fast and slow formation of four-helix bundles Configurational entropy and mechanical properties of cross-linked polymer chains: implications for protein and RNA folding.Absolute comparison of simulated and experimental protein-folding dynamics.Tuning the free-energy landscape of a WW domain by temperature, mutation, and truncation.Determination of barrier heights and prefactors from protein folding rate data Spectroscopic studies of protein folding: linear and nonlinear methods Bioinspired laser-operated molecular locomotive.Nanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides.Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediate.Mapping the energy landscape of biomolecules using single molecule force correlation spectroscopy: theory and applications Folding and unfolding of a photoswitchable peptide from picoseconds to microseconds.Loop dependence of the stability and dynamics of nucleic acid hairpins.Kinetics of contact formation and end-to-end distance distributions of swollen disordered peptides Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Coordinate-dependent diffusion in protein folding.Folding a protein in a computer: an atomic description of the folding/unfolding of protein A.A speed limit for conformational change of an allosteric membrane protein.Probing the non-native H helix translocation in apomyoglobin folding intermediates.The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods.Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequences How the folding rate constant of simple, single-domain proteins depends on the number of native contacts Extremely slow intramolecular diffusion in unfolded protein L Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions.Primary folding dynamics of sperm whale apomyoglobin: core formation Folding lambda-repressor at its speed limit.Quantitative comparison of villin headpiece subdomain simulations and triplet-triplet energy transfer experiments Determining intrachain diffusion coefficients for biopolymer dynamics from single-molecule force spectroscopy measurements.Universality in the timescales of internal loop formation in unfolded proteins and single-stranded oligonucleotides.Dynamics, energetics, and structure in protein folding An amino acid code for protein folding Folding, misfolding, and amyloid protofibril formation of WW domain FBP28.

P2860

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P2860

Measuring the rate of intramolecular contact formation in polypeptides.

http://www.wikidata.org/entity/Q35155346

description

2000 nî lūn-bûn

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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հունիսին հրատարակված գիտական հոդված

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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年論文

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2000年論文

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2000年论文

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name

Measuring the rate of intramolecular contact formation in polypeptides.

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Measuring the rate of intramolecular contact formation in polypeptides.

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Measuring the rate of intramolecular contact formation in polypeptides.

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Measuring the rate of intramolecular contact formation in polypeptides.

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Measuring the rate of intramolecular contact formation in polypeptides.

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Measuring the rate of intramolecular contact formation in polypeptides.

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PNAS.97.13.7220

P1433

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

P1476

Measuring the rate of intramolecular contact formation in polypeptides.

@en

P2093

J Hofrichter

http://www.w3.org/2001/XMLSchema#string

L J Lapidus

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W A Eaton

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P2860

DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS

Stability of alpha-helices

Distance dependence of the tryptophan-disulfide interaction at the triplet level from pulsed phosphorescence studies on a model system.

Stability of α-Helices

Phosphorescence lifetime of tryptophan in proteins.

Comparison of the time-resolved absorption and phosphorescence from the tryptophan triplet state in proteins in solution.

Fast kinetics and mechanisms in protein folding.

Intra and intermolecular charge effects on the reaction of the superoxide radical anion with semi-oxidized tryptophan in peptides and N-acetyl tryptophan.

Temperature dependence of the disulfide perturbation to the triplet state of tryptophan

Diffusion in a rough potential

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7220-7225

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scholarly article

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10.1073/PNAS.97.13.7220

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13

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