A helix-turn-strand structural motif common in alpha-beta proteins.
about
The TIM-barrel fold: a versatile framework for efficient enzymesStructure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin.Mining protein loops using a structural alphabet and statistical exceptionalityThermoregulated expression and characterization of an NAD(P)H-dependent 2-cyclohexen-1-one reductase in the plant pathogenic bacterium Pseudomonas syringae pv. glycinea.The importance of surface loops for stabilizing an eightfold beta alpha barrel protein.Conformational analysis and clustering of short and medium size loops connecting regular secondary structures: a database for modeling and prediction.Evolution of parallel beta/alpha-barrel enzyme family lightened by structural data on starch-processing enzymes.Structural aspects of protein-DNA recognition.Linkers of secondary structures in proteins.The antigenic domain of flagellin from S. paratyphi shares a structural fold with subtilisin.Modeling Loops in Protein Structures
P2860
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P2860
A helix-turn-strand structural motif common in alpha-beta proteins.
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
A helix-turn-strand structural motif common in alpha-beta proteins.
@ast
A helix-turn-strand structural motif common in alpha-beta proteins.
@en
type
label
A helix-turn-strand structural motif common in alpha-beta proteins.
@ast
A helix-turn-strand structural motif common in alpha-beta proteins.
@en
prefLabel
A helix-turn-strand structural motif common in alpha-beta proteins.
@ast
A helix-turn-strand structural motif common in alpha-beta proteins.
@en
P2093
P356
P1433
P1476
A helix-turn-strand structural motif common in alpha-beta proteins.
@en
P2093
P2860
P304
P356
10.1002/PROT.340080407
P407
P577
1990-01-01T00:00:00Z