(Q36393227)

English

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

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 August 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 (English)

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

1 reference

based on heuristic

inferred from title

author name string

Xiaoyan Yang

1

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Ramakrishna Vadrevu

2

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Ying Wu

3

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

C Robert Matthews

4

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

publication date

1 July 2007

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

16

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

7

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

1398-1409

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

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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Hydrogen exchange methods to study protein folding

1 reference

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2206699

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A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase

1 reference

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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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2206699

30 September 2017

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

1 reference

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30 September 2017

Hydrogen bonding stabilizes globular proteins

1 reference

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Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2

1 reference

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Satisfying hydrogen bonding potential in proteins

1 reference

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Hydrogen exchange and structural dynamics of proteins and nucleic acids

2 references

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30 September 2017

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

1 reference

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Helix signals in proteins

1 reference

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Strength and co-operativity of contributions of surface salt bridges to protein stability

1 reference

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The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

1 reference

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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect

1 reference

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An active proteolytic derivative of the .alpha. subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments

1 reference

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Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone.

1 reference

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Protein folding intermediates: native-state hydrogen exchange

1 reference

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Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry

1 reference

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Salt-bridges can stabilize but do not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1.

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Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein

1 reference

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A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein

1 reference

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Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein

1 reference

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21 October 2018

Identifiers

10.1110/PS.062704507

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

ResearchGate publication ID

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