Integral membrane proteins in nanoscience and synthetic biology
Nearly 30% of the proteins in a cell reside within the confines of a lipid membrane. Can we exploit the properties of these integral membrane proteins to develop new approaches in the emerging fields of biological nanoscience and synthetic biology?
Our initial target is a unique family of membrane proteins found in the diatoms. Diatoms are unicellular algae that sheath themselves in an intricate outer cell wall made of silica glass. To build this ‘glass house’, diatoms need to harvest a soluble form of silica, silicic acid, from the environment outside the cell. To do this they have evolved a novel type of integral membrane protein that can transport silicic acid across the cell membrane envelope.
We are conducting the first biochemical and biophysical studies of these silicon transporters to try and understand their structure and function at the molecular level. By reconstituting these transporters into synthetic lipid vesicles, we aim to construct a model of a simple diatom cell and use this as a new type of nanoreactor that can be used to make silica structures at nanometre length scale.
Curnow P, Senior L, Knight MJ, Thamatrakoln K, Hildebrand M, Booth PJ. (2012) Expression, purification and reconstitution of a diatom silicon transporter. Biochemistry. 51: 3776-3785.
Curnow P, Booth PJ. (2011) Φ-value analysis reveals a polarized transition state in the folding of an integral membrane protein. PNAS USA. 108(34): 14133-14138.
Curnow P, Booth PJ. (2010) The retinal cofactor controls the kinetic stability of the integral membrane protein bacteriorhodopsin. Journal of Molecular Biology. 403(4): 630-642.
Curnow P, Booth PJ. (2009) The transition state for integral membrane protein folding. PNAS USA. 106(3): 773-778.