Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding (Q30418907)

21 June 2017

title

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

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21 June 2017

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3

Schmid FX

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21 June 2017

Odefey C

1

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21 June 2017

Mayr LM

series ordinal

2

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21 June 2017

language of work or name

English

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publication date

1 January 1995

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Journal of Molecular Biology

21 June 2017

published in

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21 June 2017

volume

245

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21 June 2017

issue

1

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21 June 2017

page(s)

69-78

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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

21 June 2017

cites work

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Cis-trans equilibrium and kinetic studies of acetyl-L-proline and glycyl-L-proline

7 January 2021

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Solvent Effects on the Energetics of Prolyl Peptide Bond Isomerization

7 January 2021

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Unfolding and refolding of the constant fragment of the immunoglobulin light chain

7 January 2021

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Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray study

7 January 2021

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Analysis of the steric strain in the polypeptide backbone of protein molecules

7 January 2021

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A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model.

7 January 2021

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Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1

7 January 2021

1 reference

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Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization

7 January 2021

1 reference

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Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions

7 January 2021

1 reference

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Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding

7 January 2021

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Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate

7 January 2021

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Influence of proline residues on protein conformation

7 January 2021

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Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution

7 January 2021

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A purification method for labile variants of ribonuclease T1

7 January 2021

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Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis-proline 39 by alanine.

7 January 2021

1 reference

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Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine.

7 January 2021

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

7 January 2021

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Expression of the chemically synthesized gene for ribonuclease T1 in Escherichia coli using a secretion cloning vector.

7 January 2021

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Influences of solvent water on protein folding: free energies of solvation of cis and trans peptides are nearly identical

7 January 2021

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An explanation for the rare occurrence of cis peptide units in proteins and polypeptides

7 January 2021

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Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions

7 January 2021

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The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration

7 January 2021

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The refolding of cis- and trans-peptidylprolyl isomers of barstar

7 January 2021

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Occurrence and role of cis peptide bonds in protein structures

7 January 2021

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Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichlorophenolindophenol and potassium ferricyanide by L-ascorbic acid

7 January 2021

1 reference

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

7 January 2021

1 reference

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Energetics of ribonuclease T1 structure.

7 January 2021

1 reference

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Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2895%2980039-5

inferred from DOI database lookup

7 January 2021

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Identifiers

DOI

10.1016/S0022-2836(95)80039-5

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21 June 2017

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