Research groups

Dr Paul Curnow
Paul Curnow
Research Fellow

+44 (0)117 33 12112 (tel)
+44 (0)117 33 12168 (fax)

p.curnow@bristol.ac.uk

 

Research

diatom

A group of diatoms viewed through a polarising light microscope, highlighting the intricate glass cell wall. Credit: Spike Walker, Wellcome Images.

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.

Group

Laura Senior

Recent publications

Curnow, P. and Booth, P. J. (2011) Φ-value analysis reveals a polarized transition state in the folding of an integral membrane protein. Proc. Natl. Acad. Sci. USA. 108 (34): 14133-14138

Curnow, P. and Booth, P. J. (2010) The retinal cofactor controls the kinetic stability of the integral membrane protein bacteriorhodopsin. J. Mol. Biol. 403 (4): 630-642

Curnow, P. (2009) Membrane proteins in nanotechnology. Biochem. Soc. Transactions 37 (4): 643-652

Curnow, P. and Booth, P. J. (2009) The transition state for integral membrane protein folding. Proc. Natl. Acad. Sci. USA 106 (3): 773-778

View all publications listed on the University of Bristol's publication database