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E Steensma

Research Profile

Chemicals & Drugs

Living Beings

Azotobacter vinelandii

Physiology

Protein Folding

Phenomena

Concepts & Ideas

Disorders

Protein Denaturation

Procedures

Genes & Molecular Sequences

Amino Acid Sequences

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Publications

TOP 3
Carlo P M van Mierlo; E Steensma
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
Carlo P M van Mierlo; J M van den Oever; E Steensma
Apoflavodoxin (un)folding followed at the residue level by NMR.
Carlo P M van Mierlo; Walter M A M van Dongen; F Vergeldt; Willem J H van Berkel; E Steensma
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.

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All Publications

2000: Carlo P M van Mierlo; E Steensma
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
Journal of biotechnology 2000;79(3):281-98.
2000: Carlo P M van Mierlo; J M van den Oever; E Steensma
Apoflavodoxin (un)folding followed at the residue level by NMR.
Protein science : a publication of the Protein Society 2000;9(1):145-57.
1998: Carlo P M van Mierlo; Walter M A M van Dongen; F Vergeldt; Willem J H van Berkel; E Steensma
The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.
Protein science : a publication of the Protein Society 1998;7(11):2331-44.
1998: E Steensma; Carlo P M van Mierlo
Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.
Journal of molecular biology 1998;282(3):653-66.
1998: E Steensma; M J Nijman; Yves J M Bollen; P A de Jager; W A van den Berg; Walter M A M van Dongen; Carlo P M van Mierlo
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.
Protein science : a publication of the Protein Society 1998;7(2):306-17.
1996: E Steensma; H A Heering; Wilfred R Hagen; Carlo P M van Mierlo
Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.
European journal of biochemistry / FEBS 1996;235(1-2):167-72.

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