Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.
about
General mechanism of two-state protein folding kinetics.Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.Frustration in biomoleculesA disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBαCapturing coevolutionary signals inrepeat proteins.
P2860
Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.
description
2009 nî lūn-bûn
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name
Predicting repeat protein fold ...... ined folding energy landscape.
@en
Predicting repeat protein fold ...... ined folding energy landscape.
@nl
type
label
Predicting repeat protein fold ...... ined folding energy landscape.
@en
Predicting repeat protein fold ...... ined folding energy landscape.
@nl
prefLabel
Predicting repeat protein fold ...... ined folding energy landscape.
@en
Predicting repeat protein fold ...... ined folding energy landscape.
@nl
P2860
P356
P1433
P1476
Predicting repeat protein fold ...... ined folding energy landscape.
@en
P2093
Timothy O Street
P2860
P356
10.1002/PRO.9
P50
P577
2009-01-01T00:00:00Z