Molecular mechanism of skeletal and cardiac muscle regulatory proteins in health and diseases.

Thin filament actin binding proteins are a family of protein that binds the ubiquitous protein actin. They include tropomyosin and troponin in skeletal and cardiac muscle and tropomyosin, caldesmon and calponin in smooth muscle. They are involved in a number of cellular functions including regulation of contractility and cytoskeletal organisation and dynamics. We use a number of biochemical and biophysical techniques to investigate their structure-function relationship and how a number of disease causing mutations found in these proteins alter their function and lead to cardiomyopathies and skeletal muscle myopathies.

The PhD research area includes the biochemical basis of hypertrophic and dilated cardiomyopsathies, the structure-function relationship of the actin binding protein calponin, and investigates tropomyosin mutations involved in skeletal muscle myopathies.

Phd students are exposed to a range of techniques used in the lab including biochemical techniques (fast reaction kinetics such as stopped-flow and quenched-flow techniques, protein purification, various actin binding assays....), biophysical techniques (such as fluorescence spectroscopy), molecular biology techniques (such as cloning of protein fragments, mutagenesis...).

For further details visit our website on http://www.le.ac.uk/biochem/staff/mem16/mem16.html

We are an equal opportunities employer and particularly welcome applications for Ph.D. places from women, minority ethnic and other under-represented groups.