Sequential unfolding of the two-domain protein Pseudomonas stutzeri cytochrome c(4). (Q43919692)

28 November 2017

title

Sequential unfolding of the two-domain protein Pseudomonas stutzeri cytochrome c(4). (English)

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28 November 2017

Pseudomonas stutzeri

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Niels H Andersen

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28 November 2017

Allan Nørgaard

series ordinal

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28 November 2017

Thomas J Jensen

series ordinal

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28 November 2017

Jens Ulstrup

series ordinal

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28 November 2017

publication date

1 February 2002

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Journal of Inorganic Biochemistry

28 November 2017

published in

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28 November 2017

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28 November 2017

issue

3-4

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28 November 2017

page(s)

316-327

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Identification of the Predominant Non-Native Histidine Ligand in Unfolded Cytochrome c

28 November 2017

cites work

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Acid-induced unfolding and refolding transitions of cytochrome c: a three-state mechanism in H2O and D2O.

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A stable, molten-globule-like cytochrome c.

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CytochromecFolding and Unfolding: A Biphasic Mechanism

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Protein folding intermediates: native-state hydrogen exchange

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Following protein folding in real time using NMR spectroscopy

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Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding

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Kinetic intermediates in the formation of the cytochrome c molten globule

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Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy

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Cytochrome c folding triggered by electron transfer

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Protein folding triggered by electron transfer

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Watching protein folding unfold

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Protein Folding Triggered by Electron Transfer

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7 January 2021

Folding of cytochrome c initiated by submillisecond mixing

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A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c

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Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.

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A native tertiary interaction stabilizes the A state of cytochrome c

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7 January 2021

Kinetics and mechanism of the folding of cytochrome c

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7 January 2021

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

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The Soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c

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Linked thermal and solute perturbation analysis of cooperative domain interactions in proteins. Structural stability of diphtheria toxin

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7 January 2021

Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri determined at 2.2A resolution

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

Resonance Raman characterization of the di-heme protein cytochrome c4 from Pseudomonas stutzeri

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7 January 2021

Secondary structure of proteins through circular dichroism spectroscopy

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7 January 2021

Cold denaturation of proteins

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7 January 2021

10.1016/S0162-0134(01)00358-0

Identifiers

DOI

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28 November 2017

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