A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein (Q44127947)

30 November 2017

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

1 reference

30 November 2017

0 references

Ying Wu

1

1 reference

PubMed ID

12215410

30 November 2017

C Robert Matthews

series ordinal

2

1 reference

PubMed ID

12215410

30 November 2017

language of work or name

English

0 references

publication date

1 September 2002

1 reference

Journal of Molecular Biology

30 November 2017

1 reference

30 November 2017

322

1 reference

30 November 2017

7-13

1 reference

30 November 2017

1

1 reference

Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

30 November 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Possible implications of many proline residues for the kinetics of protein unfolding and refolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Acid catalysis of the formation of the slow-folding species of RNase A: Evidence that the reaction is proline isomerization

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Intermediates in the folding reactions of small proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Cis proline mutants of ribonuclease A. II. Elimination of the slow‐folding forms by mutation

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Multiple roles of prolyl residues in structure and folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Occurrence and role of cis peptide bonds in protein structures

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Influence of proline residues on protein conformation.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

7 January 2021

Peptide bonds revisited.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Non-proline cis peptide bonds in proteins.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Unfolding and refolding occur much faster for a proline-free proteins than for most proline-containing proteins

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Effects of proline mutations on the unfolding and refolding of human lysozyme: the slow refolding kinetic phase does not result from proline cis-trans isomerization.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Effects of proline mutations on the folding of staphylococcal nuclease.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reaction

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase alpha subunit.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Nucleotide sequences of trpA of Salmonella typhimurium and Escherichia coli: an evolutionary comparison

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Prediction of secondary structure by evolutionary comparison: application to the alpha subunit of tryptophan synthase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Pathways of protein folding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Generation of a Non-prolyl cis Peptide Bond in Ribonuclease T1

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2802%2900737-4

10.1016/S0022-2836(02)00737-4

7 January 2021

Identifiers

DOI

1 reference

30 November 2017

1 reference

PubMed ID

12215410