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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 (Q42540171)

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scientific article published on 14 September 2007

Language	Label	Description	Also known as
English	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	scientific article published on 14 September 2007

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

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 (English)

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

protein folding

0 references

author name string

Zhenyu Gu

1

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Maithreyi K Rao

2

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

William R Forsyth

3

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

John M Finke

4

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

C Robert Matthews

5

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

language of work or name

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publication date

14 September 2007

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Europe PubMed Central

PMC publication ID

2 November 2017

number of pages

19

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based on heuristic

inferred from page(s)

Journal of Molecular Biology

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Europe PubMed Central

PMC publication ID

2 November 2017

374

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

2

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

528-546

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase

1 reference

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Folding and unfolding of gammaTIM monomers and dimers

1 reference

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Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus

1 reference

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A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein

1 reference

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Stability of globular proteins in H2O and D2O.

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The folding energy landscape of the dimerization domain of Escherichia coli Trp repressor: a joint experimental and theoretical investigation

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Multiple routes lead to the native state in the energy landscape of the beta-trefoil family

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

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Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein

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

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Absence of a stable intermediate on the folding pathway of protein A.

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

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Denaturants can accelerate folding rates in a class of globular proteins

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Kinetics of Cytochrome c Folding Examined by Hydrogen Exchange and Mass Spectrometry

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Amide protection in an early folding intermediate of cytochrome c

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Identifiers

10.1016/J.JMB.2007.09.024

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

2 November 2017

ResearchGate publication ID

0 references

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