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apoflavodoxin

 
National Institutes of Health

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Highly Cited
2009
Highly Cited
2009
Protein dynamics in cells may be different from those in dilute solutions in vitro, because the environment in cells is highly… Expand
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Highly Cited
2008
Highly Cited
2008
To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding… Expand
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Highly Cited
2007
Highly Cited
2007
To investigate the consequences of macromolecular crowding on the behavior of a globular protein, we performed a combined… Expand
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2006
2006
Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and… Expand
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2004
2004
The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an alpha-beta parallel topology, have… Expand
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2003
2003
Molecular recognition begins when two molecules approach and establish interactions of certain strength. The mechanisms of… Expand
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2000
2000
Many flavoproteins are non-covalent complexes between FMN and an apoprotein. To understand better the stability of flavoproteins… Expand
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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… Expand
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1996
1996
Flavodoxins are alpha/beta proteins that mediate electron transfer reactions. The conformational stability of apoflavodoxin from… Expand
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Highly Cited
1981
Highly Cited
1981
Rat liver microsomal NADPH-cytochrome P-450 reductase was prepared free of detectable amounts of FMN by a new procedure based on… Expand
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