The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate (Q42174587)

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6 December 2019

title

The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate (English)

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6 December 2019

main subject

Azotobacter vinelandii

object named as

Azotobacter vinelandii

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inferred from title

author

Carlo P.M. van Mierlo

1

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6 December 2019

author name string

van Dongen WM

2

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6 December 2019

Vergeldt F

3

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6 December 2019

van Berkel WJ

4

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6 December 2019

Steensma E

5

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publication date

1 November 1998

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6 December 2019

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6 December 2019

volume

7

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6 December 2019

issue

11

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6 December 2019

page(s)

2331-2344

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Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.

6 December 2019

cites work

1 reference

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

26 October 2017

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Isolation, sequencing, and mutagenesis of the nifF gene encoding flavodoxin from Azotobacter vinelandii.

26 October 2017

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Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

26 October 2017

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

26 October 2017

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Tertiary structure of two-electron reduced Megasphaera elsdenii flavodoxin and some implications, as determined by two-dimensional 1H-NMR and restrained molecular dynamics

26 October 2017

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26 October 2017

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The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor

26 October 2017

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Conformational stability of apoflavodoxin

26 October 2017

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Flavine-protein interactions in flavoenzymes. Temperature-jump and stopped-flow studies of flavine analog binding to the apoprotein of Azotobacter flavodoxin

29 May 2018

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Characterization of three different flavodoxins from Azotobacter vinelandii.

29 May 2018

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Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster

29 May 2018

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29 May 2018

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29 May 2018

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17 August 2018

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12 December 2020

Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology

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12 December 2020

Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states

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A free radical flavoprotein from Azotobacter. Isolation, crystallization, and properties

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12 December 2020

Flavoprotein chemistry. II. Chemical and physical characterization of the Shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavine analog binding to the apoprotein

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12 December 2020

Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii

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12 December 2020

Interdomain interactions between the hydrophilic domains of the mannitol transporter of Escherichia coli in the unphosphorylated and phosphorylated states

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12 December 2020

Identifiers

DOI

10.1002/PRO.5560071110

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6 December 2019

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6 December 2019

PubMed publication ID

9827999

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