Dr Agata Rekas

Protein Chemist
Phone - +61 2 9717 3259
Agata Rekas staff profile


Agata is working as a Protein Chemist with the National Deuteration Facility, responsible for protein deuteration and characterization. As a biologist, she has experience in biochemistry and cell biology research, including several years of using NMR in cell biology, medicine and protein biochemistry.  She used NMR, X-ray crystallography, and more recently small-angle scattering techniques for structural and functional characterization of proteins.  Her research interests involve the role of macromolecules in human conformational diseases, and their prevention.
Academic qualifications / positions held
  • M.Sc (1993):  Jagiellonian University, Krakow, Poland - Molecular Biology “The effect of disulfide bonds on the stability of the structure of the riboflavin-binding site in the RBP (riboflavin-binding protein)”
  • Ph.D (2000):  University of Sydney, Australia - NMR, Cancer Medicine “Application of magnetic resonance spectroscopy in tumour pathology” 
  • Research associate - University of Sydney, Australia.  1998 - 1999
  • Postdoctoral fellow: Dept. of Medical Biophysics, Ontario Cancer Institute, University of Toronto, Canada  (2000 –2002)
  • Postdoctoral fellow: Department of Chemistry, University of Wollongong, Australia (2002-2006)

Selected publications

McIntosh, L., Whitelaw, C., Rekas, A., Holt, S. A., and van der Walle, C. F. (2015) Interrogating protonated/deuterated fibronectin fragment layers adsorbed to titania by neutron reflectivity and their concomitant control over cell adhesion. Journal of the Royal Society, Interface / the Royal Society 12

Curtain, C. C., Kirby, N. M., Mertens, H. D., Barnham, K. J., Knott, R. B., Masters, C. L., Cappai, R., Rekas, A., Kenche, V. B., and Ryan, T. (2015) Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study. Molecular bioSystems 11, 190-196

Pham, C. L., Kirby, N., Wood, K., Ryan, T., Roberts, B., Sokolova, A., Barnham, K. J., Masters, C. L., Knott, R. B., Cappai, R., Curtain, C. C., and Rekas, A. (2014) Guanidine hydrochloride denaturation of dopamine-induced alpha-synuclein oligomers: a small-angle X-ray scattering study. Proteins 82, 10-21

Esposito, G., Garvey, M., Alverdi, V., Pettirossi, F., Corazza, A., Fogolari, F., Polano, M., Mangione, P. P., Giorgetti, S., Stoppini, M., Rekas, A., Bellotti, V., Heck, A. J., and Carver, J. A. (2013) Monitoring the interaction between beta2-microglobulin and the molecular chaperone alphaB-crystallin by NMR and mass spectrometry: alphaB-crystallin dissociates beta2-microglobulin oligomers. J Biol Chem 288, 17844-17858

Rekas, A., Ahn, K. J., Kim, J., and Carver, J. A. (2012) The chaperone activity of alpha-synuclein: Utilizing deletion mutants to map its interaction with target proteins. Proteins 80, 1316-1325

Treweek, T. M., Rekas, A., Walker, M. J., and Carver, J. A. (2010) A quantitative NMR spectroscopic examination of the flexibility of the C-terminal extensions of the molecular chaperones, alphaA- and alphaB-crystallin. Exp Eye Res 91, 691-699

Sokolova, A., Kealley, C. S., Hanley, T., Rekas, A., and Gilbert, E. P. (2010) Small-angle X-ray scattering study of the effect of pH and salts on 11S soy glycinin in the freeze-dried powder and solution states. Journal of agricultural and food chemistry 58, 967-974


Rekas, A., Knott, R. B., Sokolova, A., Barnham, K. J., Perez, K. A., Masters, C. L., Drew, S. C., Cappai, R., Curtain, C. C., and Pham, C. L. (2010) The structure of dopamine induced alpha-synuclein oligomers. Eur Biophys J 39, 1407-1419

Benesch, J. L., Aquilina, J. A., Baldwin, A. J., Rekas, A., Stengel, F., Lindner, R. A., Basha, E., Devlin, G. L., Horwitz, J., Vierling, E., Carver, J. A., and Robinson, C. V. (2010) The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated. Chem Biol 17, 1008-1017


Rekas, A., Lo, V., Gadd, G. E., Cappai, R., and Yun, S. I. (2009) PAMAM dendrimers as potential agents against fibrillation of alpha-synuclein, a Parkinson's disease-related protein. Macromol Biosci 9, 230-238

Ghahghaei, A., Rekas, A., Carver, J. A., and Augusteyn, R. C. (2009) Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin. Molecular vision 15, 2411-2420

Rekas, A., Jankova, L., Thorn, D. C., Cappai, R., and Carver, J. A. (2007) Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species. Febs J 274, 6290-6304

Ghahghaei, A., Rekas, A., Price, W. E., and Carver, J. A. (2007) The effect of dextran on subunit exchange of the molecular chaperone alphaA-crystallin. Biochimica et biophysica acta 1774, 102-111

Treweek, T. M., Rekas, A., Lindner, R. A., Walker, M. J., Aquilina, J. A., Robinson, C. V., Horwitz, J., Perng, M. D., Quinlan, R. A., and Carver, J. A. (2005) R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. The FEBS journal 272, 711-724

Thorn, D. C., Meehan, S., Sunde, M., Rekas, A., Gras, S. L., MacPhee, C. E., Dobson, C. M., Wilson, M. R., and Carver, J. A. (2005) Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. Biochemistry 44, 17027-17036

Rekas, A., Adda, C. G., Andrew Aquilina, J., Barnham, K. J., Sunde, M., Galatis, D., Williamson, N. A., Masters, C. L., Anders, R. F., Robinson, C. V., Cappai, R., and Carver, J. A. (2004) Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity. Journal of molecular biology 340, 1167-1183


Carver, J. A., Rekas, A., Thorn, D. C., and Wilson, M. R. (2003) Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function? IUBMB Life 55, 661-668


Rekas, A., Alattia, J. R., Nagai, T., Miyawaki, A., and Ikura, M. (2002) Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity. The Journal of biological chemistry 277, 50573-50578