Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme
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Directed evolution of an E. coli inner membrane transporter for improved efflux of biofuel moleculesFirst- and second-shell metal binding residues in human proteins are disproportionately associated with disease-related SNPs.From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymesInsights into an evolutionary strategy leading to antibiotic resistance.Use of magnetic circular dichroism to study dinuclear metallohydrolases and the corresponding biomimetics.
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Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme
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im Juli 2010 veröffentlichter wissenschaftlicher Artikel
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scientific article published on 01 July 2010
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wetenschappelijk artikel
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наукова стаття, опублікована в липні 2010
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name
Mutation of outer-shell residu ...... on strength in a metalloenzyme
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Mutation of outer-shell residu ...... on strength in a metalloenzyme
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type
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Mutation of outer-shell residu ...... on strength in a metalloenzyme
@en
Mutation of outer-shell residu ...... on strength in a metalloenzyme
@nl
prefLabel
Mutation of outer-shell residu ...... on strength in a metalloenzyme
@en
Mutation of outer-shell residu ...... on strength in a metalloenzyme
@nl
P2093
P2860
P50
P356
P1433
P1476
Mutation of outer-shell residu ...... on strength in a metalloenzyme
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P2093
David L Ollis
Hye-Kyung Kim
Lawrence R Gahan
Paul D Carr
P2860
P304
P356
10.1042/BJ20100233
P407
P577
2010-07-01T00:00:00Z