apoflavodoxin

 
National Institutes of Health

Topic mentions per year

Topic mentions per year

1971-2018
0519712018

Papers overview

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2009
2009
Protein dynamics in cells may be different from those in dilute solutions in vitro, because the environment in cells is highly… (More)
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2008
2008
To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding… (More)
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2006
2006
Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and… (More)
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2004
2004
The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an alpha-beta parallel topology, have… (More)
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2001
2001
The folding reaction of Anabaena apoflavodoxin has been studied by stopped-flow kinetics and site-directed mutagenesis. Although… (More)
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2001
2001
The structure and energetics of protein-folding intermediates are poorly understood. We have identified, in the thermal unfolding… (More)
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2000
2000
Many flavoproteins are non-covalent complexes between FMN and an apoprotein. To understand better the stability of flavoproteins… (More)
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1999
1999
Anabaena apoflavodoxin contains a single histidine residue (H34) that interacts with two aromatic residues (F7 and Y47). The… (More)
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1998
1998
A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins… (More)
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1996
1996
Flavodoxins are alpha/beta proteins that mediate electron transfer reactions. The conformational stability of apoflavodoxin from… (More)
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