Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.
about
Can morphing methods predict intermediate structures?Cellular function and molecular structure of ecto-nucleotidases.Optimized torsion-angle normal modes reproduce conformational changes more accurately than cartesian modes.Conformationally gated metal uptake by apomanganese superoxide dismutase.Characterization of the Domain Orientations of E. coli 5'-Nucleotidase by Fitting an Ensemble of Conformers to DEER Distance Distributions.CDP-alcohol hydrolase, a very efficient activity of the 5'-nucleotidase/UDP-sugar hydrolase encoded by the ushA gene of Yersinia intermedia and Escherichia coli.Ecto-5'-nucleotidase: Structure function relationshipsCrystallization and preliminary X-ray analysis of the open form of human ecto-5'-nucleotidase (CD73)Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation.Contribution of the two domains of E. coli 5'-nucleotidase to substrate specificity and catalysis.Minimum action transition paths connecting minima on an energy surface.Trapped intermediate state of plant pyruvate phosphate dikinase indicates substeps in catalytic swiveling domain mechanism.
P2860
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P2860
Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.
description
2004 nî lūn-bûn
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
@zh-hk
2004年論文
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2004年論文
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2004年论文
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name
Trapping a 96 degrees domain r ...... engineered disulfide bridges.
@en
type
label
Trapping a 96 degrees domain r ...... engineered disulfide bridges.
@en
prefLabel
Trapping a 96 degrees domain r ...... engineered disulfide bridges.
@en
P2093
P2860
P356
P1433
P1476
Trapping a 96 degrees domain r ...... engineered disulfide bridges.
@en
P2093
Norbert Sträter
Robert Schultz-Heienbrok
Timm Maier
P2860
P304
P356
10.1110/PS.04629604
P577
2004-07-01T00:00:00Z