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Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.

Changes in subunit interaction energies linked to the allosteric transition of the regulatory enzyme aspartate transcarbamoylase (ATCase; EC 2.1.3.2) from Escherichia coli are localized in part at interfaces between the six catalytic (c) and six regulatory (r) polypeptide chains. Site-directed mutag...

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Hlavní autoři: Eisenstein, E, Markby, D W, Schachman, H K
Médium: Artigo
Jazyk:Inglês
Vydáno: 1989
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC287071/
https://ncbi.nlm.nih.gov/pubmed/2566165
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