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apoflavodoxin

National Institutes of Health

Papers overview

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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
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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Highly Cited
2006
Highly Cited
2006
Many native proteins occasionally form partially unfolded forms (PUFs), which can be detected by hydrogen/deuterium exchange and… Expand
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Highly Cited
2004
Highly Cited
2004
The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an alpha-beta parallel topology, have… Expand
Highly Cited
2000
Highly Cited
2000
Many flavoproteins are non-covalent complexes between FMN and an apoprotein. To understand better the stability of flavoproteins… Expand
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2000
2000
The denaturant‐induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR… Expand
Highly Cited
1998
Highly Cited
1998
A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of α/ß doubly wound proteins. The… Expand
Highly Cited
1996
Highly Cited
1996
Flavodoxins are α/β proteins that mediate electron transfer reactions. The conformational stability of apoflavodoxin from Anabœna… Expand
Highly Cited
1975
Highly Cited
1975
Abstract A method is described for determining riboflavin 5′-phosphate (FMN) and flavin adenine dinucleotide (FAD) in mixtures by… Expand