NMR structure and CD titration with metal cations of human prion alpha2-helix-related peptides.
about
Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragmentPrion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-bindingThe part of a long beta hairpin from the scrapie form of the human prion protein is reconstructed in the synthetic CC36 protein.Semisynthetic prion protein (PrP) variants carrying glycan mimics at position 181 and 197 do not form fibrils.
P2860
NMR structure and CD titration with metal cations of human prion alpha2-helix-related peptides.
description
2007 nî lūn-bûn
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2007年の論文
@ja
2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
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2007年學術文章
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2007年學術文章
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name
NMR structure and CD titration ...... alpha2-helix-related peptides.
@ast
NMR structure and CD titration ...... alpha2-helix-related peptides.
@en
type
label
NMR structure and CD titration ...... alpha2-helix-related peptides.
@ast
NMR structure and CD titration ...... alpha2-helix-related peptides.
@en
prefLabel
NMR structure and CD titration ...... alpha2-helix-related peptides.
@ast
NMR structure and CD titration ...... alpha2-helix-related peptides.
@en
P2093
P2860
P356
P1476
NMR structure and CD titration ...... alpha2-helix-related peptides.
@en
P2093
Ettore Benedetti
Filomena Rossi
Gabriella Saviano
Luisa Ronga
Pasquale Palladino
Raffaele Ragone
Teodorico Tancredi
P2860
P356
10.1155/2007/10720
P577
2007-01-01T00:00:00Z