Our Department

Faculty Directory Header Image

Suzana Straus


Research and Teaching Interests

Membrane proteins play a very important role in many cellular processes, and account for 20-40% of the products of open reading frames of known genomes. Their association with a number of diseases [1,2] has stimulated great interest in these proteins, in particular, in understanding how they function in their native lipid environments.

Because membrane proteins are embedded in a lipid matrix, the application of routine structure determination methods, namely solution state nuclear magnetic resonance (NMR) and x-ray crystallography, is precluded. The limited number of structures of membrane proteins reported to date is evidence of the difficulty in applying these methods to such systems [3,4]. In recent years, developments in the field of solid state NMR have led to an emergence of biomolecular studies using this technique. One significant advantage of using solid state NMR to study membrane proteins is that these can be studied in native-like phospholipid environments directly [5]. A further advantage of solid state NMR is that it also allows the study of membrane protein/peptide dynamics. Information on peptide mobility can provide insight into the conformational rearrangements which are linked to the peptide's biologal activity in the membrane.

Research in my laboratory focuses on the application and development of solid state NMR methods to characterise the structure and dynamics of membrane proteins. To gain insight into membrane peptide/protein, a number of relevant systems will be studied. Specifically, studies on membrane protein/lipid and membrane protein/ligand interactions will be undertaken.

1. B.W. Morrison, J. Moorman, G. Kowdley, Y. Kobayashi, L. Jones, P. Leder, MAT-8, a novel phospholemman-like protein expressed in human breast-tumors, induces a chloride conductance in Xenopus oocytes, J. Biol. Chem., 270, 2176 (1995).
2. K. Strebel, T. Klimkait, M. A. Martin, A novel gene of HIV-1, Vpu, and its 16-kilodalton product, Science, 241, 1221 (1988).
3. M. Hartmut, Crystallization of Membrane Proteins, CRC Press, Boston, MA (1991).
4. C.H.M. Papavoine, B. Christiaans, R. Folmer, R. Konings, C.W. Hilbers, Solution structure of the M13 major coat protein in detergent micelles , J. Mol. Biol., 282, 401 (1998).
5. A.Watts, Solid-state NMR approaches for studying the interaction of peptides and proteins, Biochim. Biophys. Acta, 1376, 297 (1998).


Real name: 
Office Room Number(s): 
Chemistry E213
Office Phone Number: 
Office Hours: 
see group web page/teaching for more details
Fax Number: 

Curriculum Vitae

Royal Society Dorothy Hodgkin Research Fellow, University of Oxford, UK (2000-2002); Postdoctoral Fellow, University of Pennsylvania, USA (NSERC PDF - 1998-2000); PhD, ETH Zurich, Switzerland (NSERC PGS A and B - 1993-1998); BSc (Honours), McGill University, Canada (1993);



Cheng, J. T. J. ; Hale, J. D. ; Kindrachuk, J. ; Jessen, H. ; Elliott, M. ; Hancock, R. E. W. ; Straus, S. K. Importance Of Residue 13 And The C-Terminus For The Structure And Activity Of The Antimicrobial Peptide Aurein 2.2. Biophysical Journal 2010, 99, 2926 - 2935.
Wieczorek, M. ; Jenssen, H. ; Kindrachuk, J. ; Scott, W. R. P. ; Elliott, M. ; Hilpert, K. ; Cheng, J. T. J. ; Hancock, R. E. W. ; Straus, S. K. Structural Studies Of A Peptide With Immune Modulating And Direct Antimicrobial Activity. Chemistry & Biology (Cambridge, MA, United States) 2010, 17, 970 - 980.
Pan, J. ; C. Lai, B. ; Scott, W. R. P. ; Straus, S. K. Synthetic Fusion Peptides Of Tick-Borne Encephalitis Virus As Models For Membrane Fusion. Biochemistry 2010, 49, 287 - 296.


Cheng, J. T. J. ; Hale, J. D. ; Elliot, M. ; Hancock, R. E. W. ; Straus, S. K. Effect Of Membrane Composition On Antimicrobial Peptides Aurein 2.2 And 2.3 From Australian Southern Bell Frogs. Biophysical Journal 2009, 96, 552-565.
Beasley, C. L. ; Dwork, A. J. ; Rosoklija, G. ; Mann, J. J. ; Mancevski, B. ; Jakovski, Z. ; Davceva, N. ; Tait, A. R. ; Straus, S. K. ; Honer, W. G. Metabolic Abnormalities In Fronto-Striatal-Thalamic White Matter Tracts In Schizophrenia. Schizophrenia Research 2009, 109, 159-166.


Straus, S. K. ; Scott, W. R. P. ; Marvin, D. A. The Hand Of The Filamentous Bacteriophage Helix. European Biophysics Journal with Biophysics Letters 2008, 37, 1077-1082.
Jung, D. ; Powers, J. P. ; Straus, S. K. ; Hancock, R. E. W. Lipid-Specific Binding Of The Calcium-Dependent Antibiotic Daptomycin Leads To Changes In Lipid Polymorphism Of Model Membranes. Chemistry and Physics of Lipids 2008, 154, 120-128.
Ho, S. W. ; Jung, D. ; Calhoun, J. R. ; Lear, J. D. ; Okon, M. ; Scott, W. R. P. ; Hancock, R. E. W. ; Straus, S. K. Effect Of Divalent Cations On The Structure Of The Antibiotic Daptomycin. European Biophysics Journal with Biophysics Letters 2008, 37, 421-433.
Straus, S. K. ; Scott, W. R. P. ; Symmons, M. F. ; Marvin, D. A. On The Structures Of Filamentous Bacteriophage Ff (Fd, F1, M13). European Biophysics Journal with Biophysics Letters 2008, 37, 521-527.


Scott, W. R. P. ; Baek, S. B. ; Jung, D. ; Hancock, R. E. W. ; Straus, S. K. Nmr Structural Studies Of The Antibiotic Lipopeptide Daptomycin In Dhpc Micelles. Biochimica Et Biophysica Acta-Biomembranes 2007, 1768, 3116-3126.
Pan, Y. L. ; Cheng, J. T. J. ; Hale, J. ; Pan, J. H. ; Hancock, R. E. W. ; Straus, S. K. Characterization Of The Structure And Membrane Interaction Of The Antimicrobial Peptides Aurein 2.2 And 2.3 From Australian Southern Bell Frogs. Biophysical Journal 2007, 92, 2854-2864.


Beasley, C. L. ; Tait, A. ; Straus, S. ; Dwork, A. J. ; Honer, W. G. Metabolomic And Proteomic Investigation Of The Anterior Limb Of The Internal Capsule In Schizophrenia - Evidence For Metabolic Changes?. Biological Psychiatry 2006, 59, 113.
Straus, S. K. ; Hancock, R. E. W. Mode Of Action Of The New Antibiotic For Gram-Positive Pathogens Daptomycin: Comparison With Cationic Antimicrobial Peptides And Lipopeptides. Biochimica Et Biophysica Acta-Biomembranes 2006, 1758, 1215-1223.


Bleile, D. W. ; Scott, W. R. P. ; Straus, S. K. Can Pisema Experiments Be Used To Extract Structural Parameters For Mobile Beta-Barrels?. Journal of Biomolecular Nmr 2005, 32, 101-111.
Vaccaro, L. ; Cross, K. J. ; Kleinjung, J. ; Straus, S. K. ; Thomas, D. J. ; Wharton, S. A. ; Skehel, J. J. ; Fraternali, F. Plasticity Of Influenza Haemagglutinin Fusion Peptides And Their Interaction With Lipid Bilayers. Biophysical Journal 2005, 88, 25-36.


Straus, S. K. Recent Developments In Solid-State Magic-Angle Spinning, Nuclear Magnetic Resonance Of Fully And Significantly Isotopically Labelled Peptides And Proteins. Philosophical Transactions of the Royal Society of London Series B-Biological Sciences 2004, 359, 997-1008.
Tiong, E. A. ; Lin, C. A. ; Pan, J. ; Straus, S. K. Is The Fusion Peptide From Tick-Borne Encephalitis Virus (Tbev) A Prototype For Class Ii Fusion Proteins?. Protein Science 2004, 13, 462.


Straus, S. K. ; Scott, W. R. P. ; Watts, A. Assessing The Effects Of Time And Spatial Averaging In N-15 Chemical Shift/n-15-H-1 Dipolar Correlation Solid State Nmr Experiments. Journal of Biomolecular Nmr 2003, 26, 283-295.