Elizabeth Meiering

Professor Meiering’s research group is elucidating how the primary amino acid sequence of a protein determines its folding and function. Knowledge of the molecular mechanisms governing protein folding, dynamics and function is essential for understanding natural proteins, misfolding and toxicity of variant proteins in disease and biotechnology, and engineering or designing proteins for a great, and barely tapped, range of modern biotechnological and medical applications.

They use a multidisciplinary approach integrating complementary experimental and modelling methods, to produce, engineer, and analyze recombinant protein variants in bacteria (E. coli) using biochemical and biophysical techniques, such as: differential scanning and isothermal titration calorimetry (DSC, ITC), multi-dimensional heteronuclear NMR spectroscopy, optical spectroscopies (fluorescence, CD, FTIR), light scattering, stopped-flow rapid mixing, atomic force microscopy, and computational modelling (bioinformatics, Rosetta, molecular dynamics). They analyze diverse proteins of biological, biotechnological and medical importance.

Current projects include:
* Hisactophilin: folding and function of a model beta trefoil protein with regulated pH-dependent actin- and membrane-binding
* ThreeFoil: folding and function of a designed, symmetric, multivalent carbohydrate binding beta-trefoil protein
* Adnectins: stability and solubility of engineered target binding protein biologics
* Human Superoxide Dismutase: protein folding and aggregation toxicity in disease

A more in depth description of current research projects can be found on the Meiering group website Protein Folding Laboratory.

• Proteins: folding, misfolding and aggregation, structure, dynamics, and function
• Protein engineering and design
• Protein thermodynamics and kinetics
• Biophysical chemistry and biochemistry
• Bionanotechnology and biomaterials
• Biochemistry and Biophysics
• Smart Materials
• Biomaterials, Polymers and Bioplastics
• Theranostic Materials
• Smart and Functional Materials
• Molecular Therapeutics and Theranostics
• Nanomaterials
• Bionanotechnology and Biosensors
• Soft Matter
• Drug Discovery, Design and Delivery
• Bioinformatics, Systematics and Evolution

• 1996, Postdoctoral Research Fellow Biological Chemistry and Molecular Pharmacology, Harvard Medical School, USA
• 1992, PhD, Biological Chemistry, University of Cambridge, UK
• 1988, BSc, Honours Chemistry, Physics Option, University of Waterloo, Canada

• 2017-2019, Proteins Gordon Research Conference, Elected Vice Chair and Chair
• 2015, Outstanding Performance Award in Teaching and Scholarship, Faculty of Science
• 2014, Keynote Lecture in Symposium on Biophysical Chemistry, Canadian Society for Chemistry
• 2005-2012, University Research Chair, University of Waterloo
• 2012, Outstanding Performance Award in Teaching and Scholarship, Faculty of Science
• 2010, Award of Excellence in Graduate Supervision (Nominated), University of Waterloo
• 2009 Outstanding Performance Award in Teaching and Scholarship, Faculty of Science
• 1995, John Charles Polanyi Prize for Outstanding Research in Chemistry
• 1992-1995, Jane Coffin Child Memorial Fund for Medical Research Postdoctoral Fellowship
• 1992, Damon Runyan Walter Winchell Postdoctoral Fellowship (Declined)
• 1988-1992, NSERC 1967 Graduate Research Scholarship
• 1988-1991, United Kingdom Overseas Research Studentship

• 2005-present, Protein Engineering Design and Selection, Editorial Board Member
• 2010-2014, FAUW Representative on Amalgamated Daycare Board of Directors
• 2010-2014, CIHR BMA Peer Review Committee Member
• 2011-2013, Associate Dean Graduate Studies
• 2010-2011, Materials and Nanoscience Program Development Committee
• 2010, NIH/NINDS Grant Reviewer
• 2009-2010, UW Senate Long Range Planning
• 2006-2010, UW Senator for Faculty of Science
• 2007-2009, UW Senate Executive
• 2005-2009, ALS Society of Canada Scientific Advisory Committee and Research Policy Committee
• 2008, Working Group on Faculty Annual Performance Evaluation

• President, The Protein Society

• Member, Centre for Bioengineering and Biotechnology
• Member, Institute of Biochemistry and Molecular Biology

• Please see the Protein Folding Lab website for further information on the Meiering group’s research and publications.
• Broom, A., Ma, S.M., Xia, K., Rafalia, H., Trainor, K., Colon, W., Gosavi, S., and Meiering, E.M.* Designed protein reveals structural determinants of extreme kinetic stability. Proceedings of the National Academy of Sciences USA 112, 14605-10 (2015) (pdf).
• Broom, A., Doxey, A.C., Lobsanov, Y.D., Berthin, L.G., Rose, D.R., Howell, P.L., McConkey, B.J.*, and Meiering, E.M.* Modular evolution and the origins of symmetry: Reconstruction of a three-fold symmetric globular protein. Structure 20, 161-171 (2012) (pdf).
• Shental-Bechor, D., Smith, M.T.J., Mackenzie, D., Broom, A., Marcovitz, A., Ghashut, F., Go, C., Bralha, F., Meiering, E.M.*, and Levy, Y.* Nonnative interactions regulate folding and switching of myristoylated protein. Proceedings of the National Academy of Sciences USA 109, 17839-44 (2012) (pdf).
• Smith, M.T.J., Meissner, J., Esmonde, S., Wong, H.J., and Meiering, E.M.* Energetics and mechanisms of folding and flipping the myristoyl switch in the beta-trefoil protein, hisactophilin. Proceedings of the National Academy of Sciences USA 107, 20952-20957 (2010) (pdf).
• Trainor, K., Gingras, Z., Shillingford, C., Malakian, H., Gosselin, M., Lipovsek, D., and Meiering, E.M.* Ensemble Modeling and intracellular aggregation of an engineered immunoglobulin-like domain. J. Mol. Biol. 428, 1365-74 (2016) (pdf). Human Superoxide Dismutase: protein folding and aggregation toxicity in ALS.
• Broom, H.R., Rumfeldt, J.A.O., and Meiering, E.M.* Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis. Essays in Biochemistry 56, 149-65 (2014) (pdf).
• Sekhar, A.*, Rumfeldt, J.A., Broom, H.R., Doyle, C.M., Bouvignies, G., Meiering, E.M.*, and Kay, L.E.* Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. eLife 4, e07296/33pgs (2015) (pdf).
• Vassall, K.A., Stubbs, H.R., Primmer, H.A., Tong, M.S., Sullivan, S.M., Sobering, R., Srinivasan, S., Briere, L.A.K., Dunn, S.D., Colon, W., and Meiering, E.M.* Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. Proceedings of the National Academy of Sciences USA 108, 2210-2215 (2011) (pdf).