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Andreas Milias Argeitis on Muck Rack

Andreas Milias Argeitis

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Articles

Allostery can convert binding free energies into concerted domain motions in enzymes - Nature Communications

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By Nicole Stéphanie Galenkamp, Sarah Zernia, Andreas Milias Argeitis
| Nature Verified
Abstract Enzymatic mechanisms are typically inferred from structural data. However, understanding enzymes require unravelling the intricate dynamic interplay between dynamics, conformational substates, and multiple protein structures. Here, we use single-molecule nanopore analysis to investigate the catalytic conformational changes of adenylate kinase (AK), an enzyme that catalyzes the interconversion of various adenosine phosphates (ATP, ADP, and AMP).
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