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Issue 40, 2015
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Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective

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Abstract

Ad hoc quantum chemical modeling of the acetyl-CoA synthase local structure and folding allowed us to identify an unprecedented coordination mode of histidine sidechain to protein-embedded metal ions.

Graphical abstract: Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective

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Publication details

The article was received on 21 Feb 2015, accepted on 07 Apr 2015 and first published on 07 Apr 2015


Article type: Communication
DOI: 10.1039/C5CC01575H
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2015,51, 8551-8554
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    Influence of key amino acid mutation on the active site structure and on folding in acetyl-CoA synthase: a theoretical perspective

    C. Greco, A. Ciancetta, M. Bruschi, A. Kulesza, G. Moro and U. Cosentino, Chem. Commun., 2015, 51, 8551
    DOI: 10.1039/C5CC01575H

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