Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly (Q37579763)

21 August 2017

Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly (English)

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21 August 2017

1 reference

Labhardt AM

1

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PMCID

392214

21 August 2017

language of work or name

English

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publication date

1 December 1984

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Proceedings of the National Academy of Sciences of the United States of America

21 August 2017

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21 August 2017

81

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21 August 2017

24

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21 August 2017

7674-7678

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A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A

21 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Tertiary structure of ribonuclease

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Guanidine-unfolded state of ribonuclease A contains both fast- and slow-refolding species

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Automatic identification of secondary structure in globular proteins

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Role of proline isomerization in folding of ribonuclease A at low temperatures

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

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

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Recombination of S-peptide with S-protein during folding of ribonuclease S. II. Kinetic characterization of a stable folding intermediate shown by S-protein at pH 1.7.

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Recombination of S-peptide with S-protein during folding of ribonuclease S. I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Refolding behavior of a kinetic intermediate observed in the low pH unfolding of ribonuclease A

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

A quantitative treatment of the kinetics of the folding transition of ribonuclease A

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groups

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

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

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Circular dichroic analysis of protein conformation: inclusion of the beta-turns.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=392214

Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange

1 September 2018

1 reference

12 December 2020

Optical activity of cystine-containing proteins. II. Circular dichroism spectra of pancreatic ribonuclease A, ribonuclease S, and ribonuclease S-protein

1 reference

12 December 2020

A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A

1 reference

12 December 2020

Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide

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12 December 2020

The refined crystal structure of ribonuclease A at 2.0 A resolution

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12 December 2020

Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescence

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12 December 2020

Secondary structure in ribonuclease. I. Equilibrium folding transitions seen by amide circular dichroism

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12 December 2020

Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements

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12 December 2020

Measurement of the refolding combination reaction between S-peptide and S-protein

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12 December 2020

Determination of cis-trans proline isomerization by trypsin proteolysis. Application to a model pentapeptide and to oxidized ribonuclease A

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12 December 2020

Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S.

1 reference

12 December 2020

Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A

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12 December 2020

Isomerization of proline-93 during the unfolding and refolding of ribonuclease A

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12 December 2020

Mechanism for the unfolding and refolding of ribonuclease A. Kinetic studies utilizing spectroscopic methods

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12 December 2020

Mechanism for the unfolding and refolding of ribonuclease A. Simulations using a simple model with no structural intermediates

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12 December 2020

The active site of ribonuclease A from the crystallographic studies of ribonuclease-A-inhibitor complexes

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12 December 2020

Structure of ribonuclease A: results of joint neutron and X-ray refinement at 2.0-A resolution

1 reference

12 December 2020

A native-like intermediate on the ribonuclease A folding pathway. 1. Detection by tyrosine fluorescence changes

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.81.24.7674

1 reference

21 August 2017

0 references

1 reference

21 August 2017

1 reference

PMCID

392214