Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c. (Q34815111)

4 August 2017

title

Kinetic evidence for an on-pathway intermediate in the folding of cytochrome c. (English)

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4 August 2017

Y Bai

1

1 reference

4 August 2017

language of work or name

English

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publication date

1 January 1999

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

4 August 2017

published in

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4 August 2017

volume

96

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4 August 2017

issue

2

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4 August 2017

page(s)

477-480

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Protein folding: matching theory and experiment

4 August 2017

cites work

1 reference

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8 July 2018

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Protein folding coupled to disulphide bond formation

8 July 2018

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Ultrafast signals in protein folding and the polypeptide contracted state

8 July 2018

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Molecular collapse: the rate-limiting step in two-state cytochrome c folding

8 July 2018

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On-pathway versus off-pathway folding intermediates

8 July 2018

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8 July 2018

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Understanding how proteins fold: the lysozyme story so far.

8 July 2018

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Protein folding intermediates: native-state hydrogen exchange

8 July 2018

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Kinetic Evidence for Incorrectly Folded Intermediate States in the Refolding of Denatured Proteins

8 July 2018

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

8 July 2018

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

8 July 2018

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Transient folding intermediates characterized by protein engineering

8 July 2018

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A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range

8 July 2018

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

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions.

21 January 2018

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Multiple kinetic intermediates accumulate during the unfolding of horse cytochrome c in the oxidized state

21 January 2018

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Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea.

21 January 2018

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Evidence for an obligatory intermediate in the folding of interleukin-1 beta

21 January 2018

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A pulse-chase-competition experiment to determine if a folding intermediate is on or off-pathway: application to ribonuclease A

21 January 2018

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Nature of the fast and slow refolding reactions of iron(III) cytochrome c

21 January 2018

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The barriers in protein folding

21 January 2018

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Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands

21 January 2018

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Folding intermediates in cytochrome c

21 January 2018

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Ligand exchange during cytochrome c folding

21 January 2018

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Protein stability parameters measured by hydrogen exchange

21 January 2018

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Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation

21 January 2018

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Evidence for barrier-limited protein folding kinetics on the microsecond time scale

21 January 2018

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Protein interactions with urea and guanidinium chloride. A calorimetric study

21 January 2018

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Kinetic mechanisms of protein folding

21 January 2018

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The energetic ups and downs of protein folding

21 January 2018

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Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate

21 January 2018

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The Solubility of Amino Acids, Diglycine, and Triglycine in Aqueous Guanidine Hydrochloride Solutions

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/9892658

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/9892658

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.96.2.477

1 reference

4 August 2017

0 references

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4 August 2017

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