Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helix
about
Observing cellulose biosynthesis and membrane translocation in crystalloStructural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains.Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process.Backbone Hydrogen Bond Strengths Can Vary Widely in Transmembrane Helices.
P2860
Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helix
description
2014 nî lūn-bûn
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2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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2014年论文
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2014年论文
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name
Side-chain to main-chain hydro ...... or protein transmembrane helix
@en
type
label
Side-chain to main-chain hydro ...... or protein transmembrane helix
@en
prefLabel
Side-chain to main-chain hydro ...... or protein transmembrane helix
@en
P2093
P2860
P1433
P1476
Side-chain to main-chain hydro ...... or protein transmembrane helix
@en
P2093
Alexander Götz
Christina Scharnagl
Daniel Hornburg
Oxana Pester
Philipp Hornburg
P2860
P304
P356
10.1016/J.BPJ.2014.02.013
P407
P577
2014-03-01T00:00:00Z