The complete folding pathway of a protein from nanoseconds to microseconds. - Wikidata - awgldk - TriplyDB

The complete folding pathway of a protein from nanoseconds to microseconds.

The complete folding pathway of a protein from nanoseconds to microseconds.

http://www.wikidata.org/entity/Q33186113

about

In Silico Folding of a Three Helix Protein and Characterization of Its Free-Energy Landscape in an All-Atom Force Field Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics The helix turn helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein The High-Resolution NMR Structure of the Early Folding Intermediate of the Thermus thermophilus Ribonuclease H Engineering a two-helix bundle protein for folding studies The Plastic Energy Landscape of Protein Folding: A TRIANGULAR FOLDING MECHANISM WITH AN EQUILIBRIUM INTERMEDIATE FOR A SMALL PROTEIN DOMAIN Structural dynamics of native and V260E mutant C-terminal domain of HIV-1 integrase.Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain.The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment Formation of the folding nucleus of an SH3 domain investigated by loosely coupled molecular dynamics simulations.Inactivation and reactivation of ribonuclease A studied by computer simulation.Accelerated simulation of unfolding and refolding of a large single chain globular protein.Globally, unrelated protein sequences appear random.Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder.Full reconstruction of a vectorial protein folding pathway by atomic force microscopy and molecular dynamics simulations.The folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.Spectroscopic studies of protein folding: linear and nonlinear methods How fast is protein hydrophobic collapse?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.Prediction of structural stability of short beta-hairpin peptides by molecular dynamics and knowledge-based potentials.Refolding the engrailed homeodomain: structural basis for the accumulation of a folding intermediate Kinetics of chain motions within a protein-folding intermediate.Monitoring protein interactions and dynamics with solvatochromic fluorophores.Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation 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.Fast protein folding kinetics Testing protein-folding simulations by experiment: B domain of protein A.Kinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein.Collapse dynamics of single proteins extended by force.Conformational transition of amyloid beta-peptide.Dynameomics: a comprehensive database of protein dynamics.Microscopic reversibility of protein folding in molecular dynamics simulations of the engrailed homeodomain

P2860

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P2860

The complete folding pathway of a protein from nanoseconds to microseconds.

http://www.wikidata.org/entity/Q33186113

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

The complete folding pathway of a protein from nanoseconds to microseconds.

@ast

The complete folding pathway of a protein from nanoseconds to microseconds.

@en

type

label

The complete folding pathway of a protein from nanoseconds to microseconds.

@ast

The complete folding pathway of a protein from nanoseconds to microseconds.

@en

prefLabel

The complete folding pathway of a protein from nanoseconds to microseconds.

@ast

The complete folding pathway of a protein from nanoseconds to microseconds.

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P1433

P1476

The complete folding pathway of a protein from nanoseconds to microseconds.

@en

P2093

Christopher M Johnson

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

Darwin O V Alonso

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

Gouri S Jas

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

J Günter Grossmann

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

Nicholas R Guydosh

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

Satoshi Sato

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

Stefan M V Freund

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

P2860

Using flexible loop mimetics to extend -value analysis to secondary structure interactions

Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein.

High populations of non-native structures in the denatured state are compatible with the formation of the native folded state

The N-terminal extension of rusticyanin is not responsible for its acid stability.

Is protein folding hierarchic? II. Folding intermediates and transition states.

Is there a unifying mechanism for protein folding?

Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation

The speed limit for protein folding measured by triplet-triplet energy transfer.

Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model.

Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding

P2888

P304

863-867

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

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scholarly article

P356

10.1038/NATURE01428

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P407

P433

6925

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

P478

421

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

P50

Valerie Daggett

P577

2003-02-01T00:00:00Z

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

P6179

1024403072

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P698

12594518

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P921

protein folding