Direct single-molecule observation of a protein living in two opposed native structures. - Wikidata - awgldk - TriplyDB

Direct single-molecule observation of a protein living in two opposed native structures.

Direct single-molecule observation of a protein living in two opposed native structures.

http://www.wikidata.org/entity/Q37238717

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Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide Protein stability: computation, sequence statistics, and new experimental methods Cysteine-free rop: A four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics Structural Basis for Feed-Forward Transcriptional Regulation of Membrane Lipid Homeostasis in Staphylococcus aureus Structural plasticity of 4- -helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein Conformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer Model Interdomain Contacts Control Native State Switching of RfaH on a Dual-Funneled Landscape Evolution, energy landscapes and the paradoxes of protein folding.Protein folding at single-molecule resolution.Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Rapid mapping of interactions between Human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy.Energetics and mechanisms of folding and flipping the myristoyl switch in the {beta}-trefoil protein, hisactophilin Mechanism of activation of protein kinase JAK2 by the growth hormone receptor.Frustration in biomolecules Interdomain communication revealed in the diabetes drug target mitoNEET Forced folding of a disordered protein accesses an alternative folding landscape.Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins Folding helical proteins in explicit solvent using dihedral-biased tempering.Biomolecular dynamics: order-disorder transitions and energy landscapes Munc18-1 is a molecular chaperone for α-synuclein, controlling its self-replicating aggregation Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae A cell-free approach to accelerate the study of protein-protein interactions in vitro.Cortactin scaffolds Arp2/3 and WAVE2 at the epithelial zonula adherens.Shedding light on protein folding landscapes by single-molecule fluorescence.Multicolor single-molecule FRET to explore protein folding and binding What precision-protein-tuning and nano-resolved single molecule sciences can do for each other.Massive conformation change in the prion protein: Using dual-basin structure-based models to find misfolding pathways.Oligomerization of the tetramerization domain of p53 probed by two- and three-color single-molecule FRET.Single Pair Förster Resonance Energy Transfer: A Versatile Tool To Investigate Protein Conformational Dynamics.Exploring biomolecular energy landscapes.Revealing the global map of protein folding space by large-scale simulations.Simulation of FRET dyes allows quantitative comparison against experimental data.SOLVING SINGLE BIOMOLECULES BY ADVANCED FRET-BASED SINGLE-MOLECULE FLUORESCENCE TECHNIQUES Homodimerization regulates an endothelial specific signature of the SOX18 transcription factor

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P2860

Direct single-molecule observation of a protein living in two opposed native structures.

http://www.wikidata.org/entity/Q37238717

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 08 June 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Direct single-molecule observation of a protein living in two opposed native structures.

@en

Direct single-molecule observation of a protein living in two opposed native structures.

@nl

type

label

Direct single-molecule observation of a protein living in two opposed native structures.

@en

Direct single-molecule observation of a protein living in two opposed native structures.

@nl

prefLabel

Direct single-molecule observation of a protein living in two opposed native structures.

@en

Direct single-molecule observation of a protein living in two opposed native structures.

@nl

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P356

PNAS.0904461106

P1433

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

P1476

Direct single-molecule observation of a protein living in two opposed native structures.

@en

P2093

Alexander Schug

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

Allan Chris M Ferreon

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

Ashok A Deniz

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

Edward A Lemke

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

Jason J Lavinder

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

Thomas J Magliery

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

Yann Gambin

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

P2860

Protein folding funnels: a kinetic approach to the sequence-structure relationship

Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core

Interconversion between two unrelated protein folds in the lymphotactin native state

Structure of the ColE1 rop protein at 1.7 A resolution

The protein folding problem

The energy landscapes and motions of proteins

Funnels, pathways, and the energy landscape of protein folding: a synthesis

Theory of protein folding: the energy landscape perspective.

Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations.

Absolute comparison of simulated and experimental protein-folding dynamics.

P304

10153-10158

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scholarly article

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10.1073/PNAS.0904461106

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P407

P433

25

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106

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P577

2009-06-08T00:00:00Z

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26275978

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19506258

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protein structure

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2700882

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