Nathan Cowieson

Monash Centre for Synchrotron Science Beamline Research Fellow BSc(Hons) Biochemistry, The University of Aberdeen, UK. 1998 PhD (Biochemistry), Structural Studies of Kinetochore Proteins, The University of Edinburgh, UK. 2001 Phone +61 (3) 9902 0117 Email:Nathan.Cowieson@sync.monash.edu.au

Research interests

Nathan Cowieson gained his PhD from the University of Edinburgh, UK in 2001 for his work on the use of protein x-ray crystallography to investigate structural proteins involved in chromosome segregation. Nathan was then awarded a University of Queensland Fellowship to work in the group of Prof Jennifer Martin, where he helped set up a high-throughput structural biology facility involving cloning, expressing and characterising many hundreds of protein coding genes involved in macrophage mediated inflammatory disease. During this time Nathan became interested in using a combination of circular dichroism, chemical cross-linking and small-angle x-ray scattering to gain structural insights into proteins and protein-protein interactions that are not tractable using crystallography or NMR. Nathan was awarded an Australian Synchrotron Research Program Fellowship to continue this work. Nathan moved to Monash University in 2008, as a Beamline Fellow at the Monash Centre for Synchrotron Science, aiming to develop techniques for protein structural analysis at the Australian Synchrotron.

Current projects include:

• Structural study of the f-actin binding protein cortactin
• Developing methods for collecting synchrotron SAXS and CD data from proteins
• Using synchrotron radiation circular dichroism to studying protein:protein interactions
• De novo modelling of protein structure based on restraints from SAXS and CD data

Selected publications

Evaluating protein:protein complex formation using synchrotron radiation circular dichroism spectroscopy. Cowieson NP, Miles AJ, Robin G, Forwood JK, Kobe B, Martin JL, Wallace BA. (2007) Proteins. [Epub ahead of print]

Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36. Satoh T, Cowieson NP, Hakamata W, Ideo H, Fukushima K, Kurihara M, Kato R, Yamashita K, Wakatsuki S. (2007) J Biol Chem. 282:28246-55.

Focusing in on structural genomics: the University of Queensland structural biology pipeline. Puri M, Robin G, Cowieson N, Forwood JK, Listwan P, Hu SH, Guncar G, Huber T, Kellie S, Hume DA, Kobe B, Martin JL. (2006) Biomol Eng. 23:281-9.

Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins. Kurz M, Cowieson NP, Robin G, Hume DA, Martin JL, Kobe B, Listwan P. (2006) Protein Expr Purif. 50:68-73.

An automatable screen for the rapid identification of proteins amenable to refolding. Cowieson NP, Wensley B, Listwan P, Hume DA, Kobe B, Martin JL. (2006) Proteomics. 6:1750-7.

Modification of recombinatorial cloning for small affinity tag fusion protein construct generation. Listwan P, Cowieson N, Kurz M, Hume DA, Martin JL, Kobe B. (2005) Anal Biochem. 346:327-9.

An inflammatory role for the mammalian carboxypeptidase inhibitor latexin: relationship to cystatins and the tumor suppressor TIG1. Aagaard A, Listwan P, Cowieson N, Huber T, Ravasi T, Wells CA, Flanagan JU, Kellie S, Hume DA, Kobe B, Martin JL. (2005) Structure. 13:309-17.

Pilot studies on the parallel production of soluble mouse proteins in a bacterial expression system. Cowieson NP, Listwan P, Kurz M, Aagaard A, Ravasi T, Wells C, Huber T, Hume DA, Kobe B, Martin JL. (2005) J Struct Funct Genomics. 6:13-20.

Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis. Cowieson NP, Partridge JF, Allshire RC, McLaughlin PJ.(2000) Curr Biol. 10:517-25.