Elizabeth Meiering

• Proteins: folding, misfolding and aggregation, structure, dynamics, and function
• Protein engineering and design
• Protein thermodynamics and kinetics
• Biophysical chemistry and biochemistry
• Bionanotechnology and biomaterials

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.

Professor Meiering teaches both undergraduate and graduate courses. Course offerings have included

• Chem 123: Chemical Reactions, Equilibria and Kinetics
• Chem 237: Introductory Biochemistry
• Chem 357: Physical Biochemistry
• Chem 430: Proteins
• Chem 494: Research Project - a variety of projects are available related to our ongoingresearch. Please contact me for details.
• Chem 731: Selected Biochemistry Topics (graduate level)

ThreeFoil: folding and function of a designed, symmetric, multivalent carbohydrate binding beta-trefoil

• 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)

Hisactophilin: folding and function of a model beta trefoil protein with regulated pH-dependent actin and membrane binding

• 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).

Adnectins: stability and solubility of engineered target binding protein biologics

• 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).

Please see the Protein Folding Laboratory website for further information on the Meiering group’s research and publications.

• Proteins Gordon Research Conference, Elected Vice Chair and Chair, 2017, 2019
• Outstanding Performance Award in Teaching and Scholarship, Faculty of Science, 2016
• Keynote Lecture in Symposium on Biophysical Chemistry, Canadian Society for Chemistry, 2014
• University Research Chair, University of Waterloo, 2005-2012
• Outstanding Performance Award in Teaching and Scholarship, Faculty of Science, 2012
• Award of Excellence in Graduate Supervision (Nominated), University of Waterloo, 2010
• Outstanding Performance Award in Teaching and Scholarship, Faculty of Science, 2009
• John Charles Polanyi Prize for Outstanding Research in Chemistry, 1995
• Jane Coffin Child Memorial Fund for Medical Research Postdoctoral Fellowship, 1992-1995
• Damon Runyan Walter Winchell Postdoctoral Fellowship (declined), 1992 
• NSERC 1967 Graduate Research Scholarship, 1988-1992
• United Kingdom Overseas Research Studentship, 1988-1991

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

(Selected)

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

The following news stories have featured Professor Meiering's research:

• November 24, 2015: New insights into protein structure could change the future of biomedicine

• ​August 20, 2014: Chemist Elizabeth Meiering takes on the ALS ice bucket challenge

• Spring 2010: What’s New with SOD1. The Northern Neuron.
• Fall 2007: Solving the Misfolded Protein Mystery. The Northern Neuron. 

1992-1996 Postdoctoral Research Fellow in Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, USA

1992 PhD in Biological Chemistry, University of Cambridge, England

1988 BSc in Honours Chemistry, Physics Option, University of Waterloo, Canada