Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
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Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJLigand binding specificity of the Escherichia coli periplasmic histidine binding protein, HisJ.On the molecular basis of the high affinity binding of basic amino acids to LAOBP, a periplasmic binding protein from Salmonella typhimurium.A genetically encoded toolkit for tracking live-cell histidine dynamics in space and time.Role of cis-trans proline isomerization in the function of pathogenic enterobacterial Periplasmic Binding Proteins.
P2860
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
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2013 nî lūn-bûn
@nan
2013 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
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Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
@ast
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
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label
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
@ast
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
@en
prefLabel
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
@ast
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.
@en
P2093
P2860
P356
P1433
P1476
Molecular dynamics simulations reveal that apo-HisJ can sample a closed conformation
@en
P2093
P2860
P304
P356
10.1002/PROT.24396
P407
P577
2013-10-17T00:00:00Z