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Synthetic phosphorylation of kinases for functional studies in vitro

Abstract:

The activity of protein kinases is heavily dependent on the phosphorylation state of the protein. Kinase phosphorylation states have been prepared through biological or enzymatic means for biochemical evaluation, but the use of protein chemical modification as an investigative tool has not been addressed. By chemically reacting a genetically encoded cysteine, phosphocysteine was installed via dehydroalanine as a reactive intermediate. The installed phosphocysteine was intended as a surroga...

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Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Organic Chemistry
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Author, Copyright Holder

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Department:
Chemistry Research Laboratory, Department of Chemistry, University of Oxford
Role:
Supervisor
Department:
Chemical Biology Group, BioTherapeutics Chemistry, WorldWide Medicinal Chemistry, Pfizer, 200 Cambridge Park Drive, Cambridge Massachusetts 01890, United States
Role:
Supervisor
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Grant:
DM4920 SOF S4731
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Project
Type of award:
DPhil
Awarding institution:
University of Oxford

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