Folding of a dimeric beta-barrel: residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain.
about
Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site.A quasi-spontaneous amyloid route in a DNA binding gene regulatory domain: The papillomavirus HPV16 E2 protein.Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.Investigating the refolding pathway of human acidic fibroblast growth factor (hFGF-1) from the residual structure(s) obtained by denatured-state hydrogen/deuterium exchange
P2860
Folding of a dimeric beta-barrel: residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain.
description
2000 nî lūn-bûn
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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2000 թվականի ապրիլին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@ast
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@en
type
label
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@ast
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@en
prefLabel
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@ast
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@en
P2093
P2860
P356
P1433
P1476
Folding of a dimeric beta-barr ...... mavirus E2 DNA binding domain.
@en
P2093
P2860
P304
P356
10.1110/PS.9.4.799
P577
2000-04-01T00:00:00Z