个人简介

Liz Meiering’s research is focused on protein folding, dynamics, function, engineering and design. Her research targets understanding neurodegenerative diseases like ALS, as well as engineering proteins to understand their fundamental characteristics. She also develops proteins for applications in biotechnology, including protein drugs. Proteins: folding, misfolding and aggregation, structure, dynamics, and function Protein engineering and design Protein thermodynamics and kinetics Biophysical chemistry and biochemistry Bionanotechnology and biomaterials 2005-present Protein Engineering Design and Selection, Editorial Board Member 2011-2013 Associate Dean Graduate Studies 2010-2014 FAUW Representative on Amalgamated Daycare Board of Directors 2010-2014 CIHR BMA Peer Review Committee Member 2010-2011 Materials and Nanoscience Program Development Committee 2010 NIH/NINDS Grant Reviewer 2009-2010 UW Senate Long Range Planning 2008 Working Group on Faculty Annual Performance Evaluation 2007-2009 UW Senate Executive 2006-2010 UW Senator for Faculty of Science 2005-2009 ALS Society of Canada Scientific Advisory Committee and Research Policy Committee Member, The Protein Society 1992-1996 Postdoctoral 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

研究领域

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: structure, dynamics, folding, function, and design. High resolution nuclear magnetic resonance spectroscopy. Optical spectroscopies. Biocomputing and protein engineering. Proteins currently under invesigation include: hisactophilin (N-terminally myristoylated, and pH sensing protein); ThreeFoil (designed three-fold symmetric protein, binds multivalent carbohydrates); human superoxide dismutase (implicated in the human disease, ALS).

近期论文

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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). 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).