A thermodynamic study of the 434-repressor N-terminal domain and of its covalently linked dimers.
about
Retroevolution of lambda Cro toward a stable monomer.The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinityDNA-mediated assembly of weakly interacting DNA-binding protein subunits: in vitro recruitment of phage 434 repressor and yeast GCN4 DNA-binding domainsMultiple molecule effects on the cooperativity of protein folding transitions in simulations.Thermodynamic analysis of the unfolding and stability of the dimeric DNA-binding protein HU from the hyperthermophilic eubacterium Thermotoga maritima and its E34D mutant.AS-48: a circular protein with an extremely stable globular structure
P2860
A thermodynamic study of the 434-repressor N-terminal domain and of its covalently linked dimers.
description
1999 nî lūn-bûn
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1999年の論文
@ja
1999年学术文章
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1999年学术文章
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1999年学术文章
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1999年学术文章
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1999年学术文章
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1999年學術文章
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1999年學術文章
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1999年學術文章
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name
A thermodynamic study of the 4 ...... its covalently linked dimers.
@en
A thermodynamic study of the 4 ...... its covalently linked dimers.
@nl
type
label
A thermodynamic study of the 4 ...... its covalently linked dimers.
@en
A thermodynamic study of the 4 ...... its covalently linked dimers.
@nl
prefLabel
A thermodynamic study of the 4 ...... its covalently linked dimers.
@en
A thermodynamic study of the 4 ...... its covalently linked dimers.
@nl
P2093
P2860
P1433
P1476
A thermodynamic study of the 4 ...... its covalently linked dimers.
@en
P2093
A Simoncsits
J Ruiz-Sanz
V V Filimonov
P2860
P304
P356
10.1046/J.1432-1327.1999.00491.X
P407
P577
1999-07-01T00:00:00Z