Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story (Q33950359)

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English	Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 July 2017

Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story (English)

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Europe PubMed Central

PubMed publication ID

30 July 2017

protein folding

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Carlo P.M. van Mierlo

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ORCID Public Data File 2021

author name string

van Mierlo CP

1

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Europe PubMed Central

PubMed publication ID

30 July 2017

Steensma E

2

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Europe PubMed Central

PubMed publication ID

30 July 2017

publication date

1 May 2000

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Europe PubMed Central

PubMed publication ID

30 July 2017

Journal of Biotechnology

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Europe PubMed Central

PubMed publication ID

30 July 2017

79

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Europe PubMed Central

PubMed publication ID

30 July 2017

3

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Europe PubMed Central

PubMed publication ID

30 July 2017

281-298

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Europe PubMed Central

PubMed publication ID

30 July 2017

Principles that govern the folding of protein chains

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The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

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Primary structure effects on peptide group hydrogen exchange

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A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy

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Is protein folding hierarchic? I. Local structure and peptide folding

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Is protein folding hierarchic? II. Folding intermediates and transition states

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A glimpse of the Holy Grail?

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Population statistics of protein structures: lessons from structural classifications

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The energy landscape of a fast-folding protein mapped by Ala-->Gly substitutions

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From Levinthal to pathways to funnels

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Polymer principles and protein folding

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Understanding how proteins fold: the lysozyme story so far.

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The fundamentals of protein folding: bringing together theory and experiment

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Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution

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Hydrogen exchange and structural dynamics of proteins and nucleic acids

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Mechanisms and uses of hydrogen exchange

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Nucleation mechanisms in protein folding

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Conformational stability of apoflavodoxin

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7 January 2021

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Protein conformational stabilities can be determined from hydrogen exchange rates

1 reference

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Hydrogen Exchange in Proteins

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

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Amide hydrogen exchange and internal dynamics in the chemotactic protein CheY from Escherichia coli.

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Are there pathways for protein folding?

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Cooperative stabilization of a molten globule apoflavodoxin fragment

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Mapping the transition state and pathway of protein folding by protein engineering

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Protein superfamilies and domain superfolds

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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Kinetic role of early intermediates in protein folding

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A residue-specific NMR view of the non-cooperative unfolding of a molten globule

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Structural analysis of non-native states of proteins by NMR methods

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Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,

1 reference

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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.

1 reference

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

1 reference

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

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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

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Apoflavodoxin (un)folding followed at the residue level by NMR.

1 reference

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

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10.1016/S0168-1656(00)00244-3

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Europe PubMed Central

PubMed publication ID

30 July 2017

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PubMed publication ID

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Europe PubMed Central

PubMed publication ID

30 July 2017

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