Manual Dynamics in Enzyme Catalysis

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Simulating Enzyme Catalysis

Theses and Dissertations. Title Enzyme catalysis and dynamics in dihydrofolate reductase.


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Abstract Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate bindings, chemical conversions, and products release. Public Abstract Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate bindings, chemical conversions, and products release.

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Bibliography Includes bibliographical references pages Recommended Citation Singh, Priyanka. Included in Chemistry Commons.

Enzyme catalysis

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Ultrafast dynamics in enzyme catalysis - Sean Moran

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Grant Agency of the Czech Republic. Year from. Year to. Abstract: Enzymes are very efficient and specific natural catalysts. Their active site is often buried inside their core and connected to a solvent via transport pathways — tunnels. Geometry, physico-chemical properties and dynamics of tunnels determine the exchange rates of ligands between the active sites and a solvent that can often limit the overall catalytic efficiency.

Theodore William Richards Professor of Chemistry, Emeritus

The project aims to establish new methods to study properties and dynamics of functionally relevant tunnels. First, we will generate molecular dynamics simulations of enzymes with known relevant tunnels. Then we will develop an automated protocol and software for a time-effective analysis of the tunnel dynamics and apply them on a wide range of enzymes.