Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa. (Q36476834)

14 August 2017

Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa. (English)

1 reference

14 August 2017

Jared M Trefethen

1 reference

14 August 2017

C Nick Pace

series ordinal

1 reference

14 August 2017

J Martin Scholtz

series ordinal

1 reference

14 August 2017

David N Brems

series ordinal

1 reference

14 August 2017

3 June 2005

1 reference

14 August 2017

1 reference

14 August 2017

1 reference

14 August 2017

1 reference

14 August 2017

1934-1938

1 reference

Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa

14 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

The present view of the mechanism of protein folding

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

The effect of net charge on the solubility, activity, and stability of ribonuclease Sa

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Linear extrapolation method of analyzing solvent denaturation curves

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Increasing protein stability by altering long-range coulombic interactions

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Protein denaturation. C. Theoretical models for the mechanism of denaturation

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Determination and analysis of urea and guanidine hydrochloride denaturation curves

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Effect of salt on the urea-unfolded form of barstar probed by m value measurements

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface

28 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding

28 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state

21 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

The kinetic pathway of folding of barnase

21 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Charge-charge interactions influence the denatured state ensemble and contribute to protein stability

21 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2253365

Effect of point mutations on the folding of globular proteins

21 September 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/15937282

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Purification of Ribonucleases Sa, Sa2, and Sa3 after Expression inEscherichia coli

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/15937282

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Rational Modification of Protein Stability by the Mutation of Charged Surface Residues†

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/15937282

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1110/PS.051401905

1 reference

14 August 2017

1 reference

14 August 2017

PubMed publication ID

15937282

1 reference