Left-handed topology of super-secondary structure formed by aligned alpha-helix and beta-hairpin.
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Treble clef finger--a functionally diverse zinc-binding structural motifSuper-secondary structures involving triple-strand beta-sheets.Why are the same protein folds used to perform different functions?The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid beta-peptide from liposomes prepared from brain membrane-like lipids.
P2860
Left-handed topology of super-secondary structure formed by aligned alpha-helix and beta-hairpin.
description
1992 nî lūn-bûn
@nan
1992 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@ast
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@en
type
label
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@ast
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@en
prefLabel
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@ast
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@en
P2860
P1433
P1476
Left-handed topology of super- ...... alpha-helix and beta-hairpin.
@en
P2093
P2860
P356
10.1016/0014-5793(92)80271-H
P407
P577
1992-05-01T00:00:00Z