Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature.
about
The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.A miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.A fluid salt-bridging cluster and the stabilization of p53.Detection of native-state nonadditivity in double mutant cycles via hydrogen exchange.
P2860
Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
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2001年學術文章
@zh-hant
name
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@en
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@nl
type
label
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@en
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@nl
prefLabel
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@en
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@nl
P2860
P1433
P1476
Hydrogen exchange of the tetra ...... y denaturants and temperature.
@en
P2093
P2860
P304
P356
10.1046/J.1432-1327.2001.02414.X
P407
P577
2001-09-01T00:00:00Z