Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.
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How does symmetry impact the flexibility of proteins?Can hydroxylamine be a more potent nucleophile for the reactivation of tabun-inhibited AChE than prototype oxime drugs? An answer derived from quantum chemical and steered molecular dynamics studies.Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain.Ligand entry into the calyx of β-lactoglobulin.Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein.Binding-competent states for L-arginine in E. coli arginine repressor apoprotein.
P2860
Symmetric allosteric mechanism of hexameric Escherichia coli arginine repressor exploits competition between L-arginine ligands and resident arginine residues.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Symmetric allosteric mechanism ...... nd resident arginine residues.
@ast
Symmetric allosteric mechanism ...... nd resident arginine residues.
@en
type
label
Symmetric allosteric mechanism ...... nd resident arginine residues.
@ast
Symmetric allosteric mechanism ...... nd resident arginine residues.
@en
prefLabel
Symmetric allosteric mechanism ...... nd resident arginine residues.
@ast
Symmetric allosteric mechanism ...... nd resident arginine residues.
@en
P2093
P2860
P1476
Symmetric allosteric mechanism ...... and resident arginine residues
@en
P2093
Jannette Carey
Michael Green
Milan Melichercik
Rebecca Strawn
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000801
P577
2010-06-03T00:00:00Z