Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
about
Computing the origin and evolution of the ribosome from its structure - Uncovering processes of macromolecular accretion benefiting synthetic biologyCotranslational protein folding--fact or fiction?Directionality in protein fold prediction.Signatures of co-translational folding.Protein folding requires crowd control in a simulated cell.Rules for connectivity of secondary structure elements in protein: Two-layer αβ sandwiches.
P2860
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
description
2006 nî lūn-bûn
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2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@ast
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@en
type
label
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@ast
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@en
prefLabel
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@ast
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@en
P2860
P1433
P1476
Topological accessibility shows a distinct asymmetry in the folds of betaalpha proteins.
@en
P2093
William R Taylor
P2860
P304
P356
10.1016/J.FEBSLET.2006.08.070
P407
P577
2006-09-11T00:00:00Z