Denaturants can accelerate folding rates in a class of globular proteins. - Wikidata - awgldk - TriplyDB

Denaturants can accelerate folding rates in a class of globular proteins.

Denaturants can accelerate folding rates in a class of globular proteins.

http://www.wikidata.org/entity/Q36280141

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Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscape Salt-induced detour through compact regions of the protein folding landscape Folding without charges.Urea orientation at protein surfaces.Magnesium-dependent folding of self-splicing RNA: exploring the link between cooperativity, thermodynamics, and kinetics Redesigning the hydrophobic core of a model beta-sheet protein: destabilizing traps through a threading approach.Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics.Folding and unfolding of gammaTIM monomers and dimers.Influence of exogenous application of glutathione on rubisco and rubisco activase in heavy metal-stressed tobacco plant grown in vitro.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.Energy landscape theory for Alzheimer's amyloid beta-peptide fibril elongation.

P2860

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P2860

Denaturants can accelerate folding rates in a class of globular proteins.

http://www.wikidata.org/entity/Q36280141

description

1996 nî lūn-bûn

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1996年の論文

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

@zh-sg

1996年學術文章

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1996年學術文章

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1996年學術文章

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name

Denaturants can accelerate folding rates in a class of globular proteins.

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Denaturants can accelerate folding rates in a class of globular proteins.

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type

label

Denaturants can accelerate folding rates in a class of globular proteins.

@ast

Denaturants can accelerate folding rates in a class of globular proteins.

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prefLabel

Denaturants can accelerate folding rates in a class of globular proteins.

@ast

Denaturants can accelerate folding rates in a class of globular proteins.

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Protein Science

P1476

Denaturants can accelerate folding rates in a class of globular proteins.

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Camacho CJ

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

Thirumalai D

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P2860

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

Reexamination of the folding of BPTI: predominance of native intermediates.

Principles of protein folding--a perspective from simple exact models.

Three-state analysis of sperm whale apomyoglobin folding.

Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor

Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease.

Experimental studies of protein folding and unfolding.

Modeling the effects of mutations on the denatured states of proteins.

Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate.

Solvent denaturation and stabilization of globular proteins.

P304

1826-1832

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

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scholarly article

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10.1002/PRO.5560050908

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9

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5

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1996-09-01T00:00:00Z

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14325811

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8880906

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protein folding

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2143547

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