Molecular dynamics simulations of LysRS: an asymmetric state.
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MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and AllosteryStructural asymmetry of the terminal catalytic complex in selenocysteine synthesisPrecision active pharmaceutical ingredients are the goal.Structural states of the flexible catalytic loop of M. tuberculosis tyrosyl-tRNA synthetase in different enzyme-substrate complexes.Multiple catalytic activities of Escherichia coli lysyl-tRNA synthetase (LysU) are dissected by site-directed mutagenesis.Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins.
P2860
Molecular dynamics simulations of LysRS: an asymmetric state.
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2006 nî lūn-bûn
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2006年の論文
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Molecular dynamics simulations of LysRS: an asymmetric state.
@en
Molecular dynamics simulations of LysRS: an asymmetric state.
@nl
type
label
Molecular dynamics simulations of LysRS: an asymmetric state.
@en
Molecular dynamics simulations of LysRS: an asymmetric state.
@nl
prefLabel
Molecular dynamics simulations of LysRS: an asymmetric state.
@en
Molecular dynamics simulations of LysRS: an asymmetric state.
@nl
P356
P1433
P1476
Molecular dynamics simulations of LysRS: an asymmetric state
@en
P2093
Andrew D Miller
Samantha J Hughes
P304
P356
10.1002/PROT.20609
P407
P577
2006-03-01T00:00:00Z