Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape - Wikidata - awgldk - TriplyDB

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

http://www.wikidata.org/entity/Q34350548

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Simulations of proteins with inhomogeneous degrees of freedom: The effect of thermostats The folding energy landscape of the dimerization domain of Escherichia coli Trp repressor: a joint experimental and theoretical investigation.Evidence of discrete substates and unfolding pathways in green fluorescent protein.Capillarity theory for the fly-casting mechanism.Modulation of frustration in folding by sequence permutation.Interdomain communication revealed in the diabetes drug target mitoNEET Multiple routes lead to the native state in the energy landscape of the beta-trefoil family Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.The dual-basin landscape in GFP folding Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.Vaccinia virus virulence factor N1L is a novel promising target for antiviral therapeutic intervention.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Topological and sequence information predict that foldons organize a partially overlapped and hierarchical structure.Characterization of the unfolded state of repeat proteins.Folding and unfolding of gammaTIM monomers and dimers.Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulation.A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin

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P2860

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

http://www.wikidata.org/entity/Q34350548

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին 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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name

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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type

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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prefLabel

Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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BIOPHYSJ.105.059147

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Biophysical Journal

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape

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John M Finke

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P2860

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

Solvent viscosity dependence of the folding rate of a small protein: distributed computing study

Automated analysis of interatomic contacts in proteins

Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates.

Direct molecular dynamics observation of protein folding transition state ensemble

Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein

The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.

Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels.

Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase.

Mutagenic analysis of the interior packing of an alpha/beta barrel protein. Effects on the stabilities and rates of interconversion of the native and partially folded forms of the alpha subunit of tryptophan synthase.

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488-505

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