Characterisation of Biomolecules Project Profile

The Project is developing ANSTO's strength, skill and reputation in supporting and applying neutron and x-ray scattering techniques to characterise biomolecular structure and function, so as to forge research connections within and beyond Australia and contribute to National Research Priority 3: Frontier technologies for the fields of biotechnology, nanotechnology and photonics

Project Leader: Dr Kerie Hammerton

Objectives/aims:

• Characterisation of the role of biomolecules in biological processes by studying the relationship between macromolecular structure and function using neutron & X-ray scattering, and other complementary techniques.
• Development of expertise in biological applications of neutron and X-ray scattering by researchers at ANSTO so as to engage the bioscience community in the S.E. Asian-Pacific Region in this field.
• Utilisation of SANS, Neutron Reflectometry and SAXS for investigating the relationship between the molecular structure & function of biomaterials including proteins, biopolymers, sol-gel based biocatalysts, biominerals  and biosensors.

Project Team:
A. Duff; C. Garvey; K. Hammerton; P. Holden; A. Rekas; R. Russell; H. Wacklin; A. Whitten; K. Wilde; S. Yun: N. Blagojevic; J. Ferris; M. James; R. Knott; M. Elcombe

Achievements:

• A major focus for the Project has been the setting up of the ANSTO Biodeuteration Facility for the production, purification and characterisation of deuterated biomolecules.  Biodeuteration (replacement of hydrogen in biomolecules with deuterium) is used to enhance the visibility of biomolecules in neutron scattering experiments.

• A new development is the establishment of a National Deuteration Facility at ANSTO for both biodeuteration and chemical deuteration of a wider range of molecules, with funding contributed from the Commonwealth Government's NCRIS (National Collaborative Research Infrastructure Strategy).

• Several beamtime applications for use of overseas facilities for neutron and X-ray scattering experiments have been awarded to Project staff including: HMI Germany (Kinetic studies of red blood cell shape change); NIST USA (Structural studies of microbial inclusion bodies); NIST USA (Structure of surface-immobilised DNA monolayer); ILL France (T cell surface proteins); HMI Germany (Conformation of microbial polyesters); and LLB France (Polymer morphology of polyhydroxy butyrate/cellulose blends). Most of these applications will utilise the OPAL neutron beamlines.
  

Significant Collaborations:
Several collaborative research investigations are underway including:

• Calmodulin signalling systems with Australian Federation Fellow Professor Jill Trewhella (University of Sydney)
• Small heat shock proteins (Adelaide University)
• Hemoglobin, lipid membranes, and cellulose (Universities of Sydney, Monash and Western Sydney)
• Microbial production of biodegradable plastics (NSW University)
• Model biomembranes and T cell surface proteins (Oxford University)

• Russell, R.A., Holden, P.J., Garvey, C.J., Wilde, K.L., Hammerton, K.M. and L.J. Foster, 2006. Investigation of the phase morphology of bacterial PHA inclusion bodies by contrast variation SANS. Physica B 385-386: 859-861.
• Garvey, C.J., Knott, R.B., Searson, M. and J.P. Conroy, 2006. USANS study of wood structure    Physica B 385-386: 877-879.
• Foster, LJR; Russell, RA; Sanguanchaipaiwong, V; Stone, DJM; Hook, JM & Holden PJ., 2006. Biosynthesis and Characterisation of Deuterated Polyhydroxyoctanoate (PHO) Biomacromolecules 7: 1344-1349
• Rodgers, L.E., Holden, P.J., Knott, R.B., Finnie, K.S., Bartlett, J.R. and L.J.R. Foster, 2005. Effect of Sol-Gel Encapsulation on Enzyme Structure and Function: A Small Angle Neutron Scattering Study. J. Sol Gel Sci Tech. 33: 65-69.
• C. J. Garvey, R. B. Knott, E. Drabarek and P. W. Kuchel, 2004.The shear induced alignment of hemoglobin aggregates in human erythrocytes : small angle neutron scattering studies.  European Biophysics Journal 33: 589-595.
  

Contact Details: Dr Kerie Hammerton