Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule?
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Streptococcus pneumoniae TIGR4 Flavodoxin: Structural and Biophysical Characterization of a Novel Drug TargetFolding of proteins with a flavodoxin-like architecture.Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme.A chemical chaperone induces inhomogeneous conformational changes in flexible proteins.The mechanism of water/ion exchange at a protein surface: a weakly bound chloride in Helicobacter pylori apoflavodoxin.A simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin
P2860
Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule?
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2008 nî lūn-bûn
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2008年の論文
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name
Molten globule and native stat ...... elative to the molten globule?
@en
type
label
Molten globule and native stat ...... elative to the molten globule?
@en
prefLabel
Molten globule and native stat ...... elative to the molten globule?
@en
P2860
P1433
P1476
Molten globule and native stat ...... elative to the molten globule?
@en
P2093
P2860
P304
P356
10.1529/BIOPHYSJ.108.130153
P407
P577
2008-04-25T00:00:00Z