Benjamin Rowlinson

Unravelling the structural biology of the LIMD1 scaffold protein using novel NMR approaches

About me

I am currently a PhD student in the Lab of Dr Michael Plevin studying the structure of the protein-protein interactions made by a signalling scaffold protein. I did my undergraduate degree at the University of York in biochemistry, and my final year project involved x-ray crystallography of P450 enzymes. I then did my M.Sc by research with Professor Gideon Grogan at the University of York working on crystallography of amide bond synthetase enzymes with potential industrial applications. My current research experience has given me a passion for structural biology which led me to undertake my current PhD in order to broaden by knowledge of the field.

My project

My project aim to provide insight into the structural mechanisms of protein-protein interactions made by signalling scaffold proteins. To do this I am studying the interactions made my the scaffold protein LIMD1 which is believed to interact with both structured and unstructured partner proteins, at both structured and unstructured regions. LIMD1 acts in a diverse range of signalling pathways including: miRNA silencing, hypoxic signalling, cell fate determination, cytoskeletal organization, cell-cell adhesion, cell differentiation, proliferation and migration. It is hoped that study of the structures of interactions made by LIMD1 will inform on general mechanisms for scaffold protein partner recognition and protein interactions involving unstructured partners. Study of these structures will involve the use solution NMR spectroscopy, x-ray crystallography and biophysical assays. Advanced NMR spectroscopy techniques will be employed with the help of the industrial collaborator NMR-Bio.


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