(Q44180455)

English

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

scientific article published in October 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 November 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

protein folding

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author name string

Ying Wu

1

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

C Robert Matthews

2

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Europe PubMed Central

PubMed publication ID

30 November 2017

language of work or name

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publication date

1 October 2002

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Europe PubMed Central

PubMed publication ID

30 November 2017

Journal of Molecular Biology

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Europe PubMed Central

PubMed publication ID

30 November 2017

323

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

2

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

309-325

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G.

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Both the fast and slow refolding reactions of ribonuclease A yield native enzyme

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

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A very fast phase in the refolding of disulfide-intact ribonuclease A: implications for the refolding and unfolding pathways

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The barriers in protein folding

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Mobile reactive centre of serpins and the control of thrombosis

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Occurrence and role of cis peptide bonds in protein structures

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Influence of proline residues on protein conformation

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Peptide bonds revisited

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Non-proline cis peptide bonds in proteins.

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

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

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The X-Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides

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

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

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

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Intermediates in the folding reactions of small proteins

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

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7 January 2021

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

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7 January 2021

Proline isomerization in bovine pancreatic ribonuclease A. 1. Unfolding conditions

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Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions

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7 January 2021

Multiple roles of prolyl residues in structure and folding

1 reference

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7 January 2021

Initial denaturing conditions influence the slow folding phase of acylphosphatase associated with proline isomerization

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7 January 2021

Identification of proline residues responsible for the slow folding kinetics in pectate lyase C by mutagenesis

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7 January 2021

Folding kinetics of the protein pectate lyase C reveal fast-forming intermediates and slow proline isomerization

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7 January 2021

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

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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

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

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7 January 2021

The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase.

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7 January 2021

Catalysis of protein folding by prolyl isomerase

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Catalysis of proline isomerization during protein-folding reactions

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Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins

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Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions

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Conformational specificity of chymotrypsin toward proline-containing substrates.

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Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy

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Estimation of globular protein secondary structure from circular dichroism.

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

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Effect of point mutations on the folding of globular proteins

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Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization

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Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor

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Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase

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Effects of proline mutations on the folding of staphylococcal nuclease.

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

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Mutagenic and thermodynamic analyses of residual structure in the alpha subunit of tryptophan synthase.

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7 January 2021

Long-range interactions within a nonnative protein

1 reference

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7 January 2021

Persistence of native-like topology in a denatured protein in 8 M urea

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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

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7 January 2021

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

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Proline in alpha-helix: stability and conformation studied by dynamics simulation

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Positional preference of proline in alpha-helices

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Flexible-geometry conformational energy maps for the amino acid residue preceding a proline

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Side-chain effects on peptidyl-prolyl cis/trans isomerisation.

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7 January 2021

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

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Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels

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7 January 2021

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

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Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthase

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Prolyl isomerases: role in protein folding.

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10.1016/S0022-2836(02)00922-1

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Europe PubMed Central

PubMed publication ID

30 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

ResearchGate publication ID

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