(Q54608071)

1 June 2018

title

Tryptophan-containing alpha-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties. (English)

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1 June 2018

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Choi SG

1

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1 June 2018

O'Donnell SE

series ordinal

2

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1 June 2018

Sarken KD

series ordinal

3

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1 June 2018

Hardman JK

series ordinal

4

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1 June 2018

language of work or name

English

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publication date

1 July 1995

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1 June 2018

Journal of Biological Chemistry

number of pages

4

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based on heuristic

inferred from page(s)

published in

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1 June 2018

volume

270

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1 June 2018

issue

30

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1 June 2018

page(s)

17712-17715

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1 June 2018

The evolution of alpha/beta barrel enzymes

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Comparison of Denaturation by Guanidine Hydrochloride of the Wild Type Tryptophan Synthase α-Subunit of Escherichia coli and Two Mutant Proteins (Glu 49—Met or Gln)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Proline isomerization and the slow folding reactions of the alpha subunit of tryptophan synthase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Characterization of a slow folding reaction for the alpha subunit of tryptophan synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Role of diffusion in the folding of the alpha subunit of tryptophan synthase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Urea-induced unfolding of the alpha subunit of tryptophan synthase: one-dimensional proton NMR evidence for residual structure near histidine-92 at high denaturant concentration.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Thermal stabilities of mutant Escherichia coli tryptophan synthase α subunits

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Affinities of phosphorylated substrates for the E. coli tryptophan synthase alpha-subunit: roles of Ser-235 and helix-8' dipole.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Effects of the phenylalanine-22----leucine, glutamic acid-49----methionine, glycine-234----aspartic acid, and glycine-234----lysine mutations on the folding and stability of the alpha subunit of tryptophan synthase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Determination and analysis of urea and guanidine hydrochloride denaturation curves

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Guanidine hydrochloride induced unfolding of the alpha subunit of tryptophan synthase and of the two alpha proteolytic fragments: evidence for stepwise unfolding of the two alpha domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Characterization of the slow steps in the folding of the alpha subunit of tryptophan synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

Conformational stability of mixed disulfide derivatives of beta-lactoglobulin B

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17712

21 January 2018

Identifiers

DOI

10.1074/JBC.270.30.17712

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1 June 2018

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1 June 2018