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Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.

Proteins often require cofactors to perform their biological functions and must fold in the presence of their cognate ligands. Using circular dichroism spectroscopy. we investigated the effects of divalent metal binding upon the folding pathway of Escherichia coli RNase HI. This enzyme binds divalen...

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Bibliografische gegevens
Hoofdauteurs: Goedken, E. R., Keck, J. L., Berger, J. M., Marqusee, S.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Cold Spring Harbor Laboratory Press 2000
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2144475/
https://ncbi.nlm.nih.gov/pubmed/11106164
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