Aggregation as the basis for complex behaviour of cutinase in different denaturants
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Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.Stabilization of an α/β-Hydrolase by Introducing Proline Residues: Salicylic Acid Binding Protein 2 from Tobacco.Folding of proteins with a flavodoxin-like architecture.Non-native hydrophobic interactions detected in unfolded apoflavodoxin by paramagnetic relaxation enhancement.Interrupted hydrogen/deuterium exchange reveals the stable core of the remarkably helical molten globule of alpha-beta parallel protein flavodoxin.Thermodynamics and mechanism of cutinase stabilization by trehalose.
P2860
Aggregation as the basis for complex behaviour of cutinase in different denaturants
description
scientific article published on 30 November 2006
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wetenschappelijk artikel
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наукова стаття, опублікована в лютому 2007
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name
Aggregation as the basis for complex behaviour of cutinase in different denaturants
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Aggregation as the basis for complex behaviour of cutinase in different denaturants
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type
label
Aggregation as the basis for complex behaviour of cutinase in different denaturants
@en
Aggregation as the basis for complex behaviour of cutinase in different denaturants
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prefLabel
Aggregation as the basis for complex behaviour of cutinase in different denaturants
@en
Aggregation as the basis for complex behaviour of cutinase in different denaturants
@nl
P2093
P50
P1476
Aggregation as the basis for complex behaviour of cutinase in different denaturants
@en
P2093
Lise Giehm
Ricardo P Baptista
Søren R Kristensen
P304
P356
10.1016/J.BBAPAP.2006.11.012
P577
2006-11-30T00:00:00Z