NMR solution structure of the acylphosphatase from Escherichia coli.
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Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilisBiological function in a non-native partially folded state of a proteinMethods for structural characterization of prefibrillar intermediates and amyloid fibrils."Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications.A hydrolase from Lactobacillus sakei moonlights as a transaminase.Mechanical unfolding of acylphosphatase studied by single-molecule force spectroscopy and MD simulations.The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli.
P2860
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P2860
NMR solution structure of the acylphosphatase from Escherichia coli.
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name
NMR solution structure of the acylphosphatase from Escherichia coli.
@en
NMR solution structure of the acylphosphatase from Escherichia coli.
@nl
type
label
NMR solution structure of the acylphosphatase from Escherichia coli.
@en
NMR solution structure of the acylphosphatase from Escherichia coli.
@nl
prefLabel
NMR solution structure of the acylphosphatase from Escherichia coli.
@en
NMR solution structure of the acylphosphatase from Escherichia coli.
@nl
P2093
P50
P1476
NMR solution structure of the acylphosphatase from Escherichia coli.
@en
P2093
Gennaro Esposito
Katiuscia Pagano
Niccolò Taddei
Paolo Viglino
P2888
P304
P356
10.1007/S10858-006-9073-2
P577
2006-10-05T00:00:00Z