Hello from Michèle Loewen! I did my PhD in the lab from 1993 to 1997, studying fish antifreeze protein types I and II. However, windsurfing was another preoccupation (the 6th floor of Botterell Hall was a great vantage point to watch for wind on the lake), much to Peter’s consternation (or was it envy?)! After leaving the lab I did two PDFs, one at University of Basel (Switzerland) and a second at MIT (USA) studying bacterial rhodopsin with Nobel Laureate H G Khorana. In 2001, I joined the National Research council (NRC) in Saskatoon as a Research Officer to work on Crop Biotechnology and serve as a liaison to the Canadian Light Source.

Now my lab has moved to NRC-Ottawa in Canada’s ‘Temple of Science’ at 100 Sussex Drive where, among other topics, I work on aspects of food security like fungal disease resistance. I’m cross appointed at both Queen’s University https://dbms.queensu.ca/faculty/michele-loewen and University of Ottawa, and relish teaching BCHM841 (grad course on proteins) with Peter, as well as eating kale in his office. I have two sons, one husband and a bigger sailboat. In 2014 I re-named my boat ‘Basic Research’, a nod to Darwin, while also protesting the government’s undermining of fundamental science and muzzling of federal researchers.

‘Basic Research is what I am doing when I don’t know what I am doing’ – Wernher von Braun

Hello everyone! I did my M.Sc. in the lab from 2007 to 2009, engineering antifreeze protein and studying ice recrystallization. Keeping a few fish in the lab along with Chris Garnham, Adam Middleton and Nelson Lin (who's my husband now :D ) was also a side hobby. After leaving the lab, I joined Sanofi Pasteur in Toronto where I made whooping cough vaccines. Over the next few years, I joined the management side of vaccine operation, and this role gave me the opportunity to build and lead a team in the antigen purification platform. In 2017, I joined the new vaccine facility project (Building 100) as a Component Pertussis Downstream Lead, to support the design, construction, commissioning and qualification of the various processing equipment and facility (I've become almost half an engineer from working with the Engineering team and vendors).  Now, I have moved to a new role to complete the project phase of the new facility and transition to routine operation. It feels great knowing that what I do everyday can help to protect everyone around me from certain infectious diseases (I made the vaccine batch that went into my son when he was 2 months old - proud mommy!).  

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I studied in Peter’s lab from 2006 until 2012 where I worked in the 'antifreeze protein half' of the lab. My primary research focus was an ice-binding protein from perennial ryegrass, Lolium perenne. Solving its crystal structure capped off my thesis. I had lots of fun in Peter’s lab where I learned basic molecular biology, was given good opportunities to mentor students and write manuscripts, and also learned some more esoteric things like how to grow enormous single ice crystals. I had a blast with my colleagues and have many good memories including the ‘Box of Feelings’, our many exciting trips to the synchrotron on Long Island, the late Carl and Carla, collecting inchworms in the dead of winter, and the Grad Club.

When I finished, my partner and I decided to travel and figured why not go as far away as we possibly could? So, we brought our 2-year-old daughter, Abby, to Dunedin New Zealand where I began my postdoc. After only signing an 18-month contract, I figured we would be back in Canada before we knew it, but we (and son, Angus) are still here 9+ years later! My independently funded current research investigates how ubiquitin transfer is regulated biochemically, and I have particular interests in E2 enzymes and developing new targeted protein degradation techniques. Dunedin is a beautiful place and I highly recommend coming for a visit – as Peter did for three months in 2015!

"Greetings! I did my PhD from 2005-2010 in Peter’s lab, studying antifreeze protein structure and function, including one summer doing research in Sapporo, Japan. I also dabbled a little bit in calpain during my time in the lab (but don’t tell anyone!). I performed my post-doctoral studies at the National Institutes of Health in Bethesda Maryland under the guidance of Dr. Antonina Roll-Mecak, where I investigated the structure:function relationship of a family of tubulin modifying enzymes. I am currently a research scientist at Agriculture and Agri-Food Canada (AAFC) in London, ON, where I primarily study mycotoxin biosynthesis and detoxification. My knowledge of mycotoxins was non-existent prior to starting my lab at AAFC. However, my biochemistry and structural biology skills that I first developed in Peter’s lab were instrumental in allowing me to collaborate with my new colleagues in London and join a team whose whole is greater than the sum of its parts. I got hooked on science in Peter’s lab after I made my first big discovery there – solving the X-ray crystal structure of a novel bacterial antifreeze protein that turned out to be an ice adhesin – and I’ve been chasing that high ever since. Some things never get old!"

Hello! I did my PhD studies in the Davies lab from 2010-2016. I had the opportunity to purify and characterize native antifreeze protein from the infamous Kingston midges. This proved to be a novel antifreeze type with an ice-binding site made up of stacked tyrosines. I'm pretty sure my PhD thesis was the 'coolest' of all time! Not only was the work incredibly interesting, but it also set me up for a career in protein science. My thesis project involved mass spectrometry, recombinant protein production, molecular biology, and structural biology. With the training I had in the Davies lab from Peter, Laurie, Sherry, Rob, Qilu, and my labmates, I am confident in my biochemistry foundations. After graduating from Queen's, I joined the Craik Lab at UCSF as a postdoc, where I continued to study interesting and challenging proteins. All the techniques I learned from my academic background are proving useful in my current role. I am a scientist in the Protein Science team at Frontier Medicines, a rapidly growing biotech company in the Bay Area. We are developing small molecule drugs for difficult but pertinent cancer proteins. I've been living in the Bay Area since 2016 with my husband and daughter and feel incredibly grateful to have such an interesting job as a scientist!

Hi there! After working in Peter’s lab as a summer student during my undergraduate studies at Queen’s, I stayed on to complete a Master’s degree from 2015-2017. My project focused on the multimerization of antifreeze proteins to increase their activity, which we accomplished by genetically fusing AFPs to the subunits of self-assembling protein cages produced by the David Baker lab at U. Wash.

I have worked in several roles in the biotech industry since finishing my degree at Queen’s, and it has never been a dull moment! Recently, I completed a stint as a consultant at Sanofi Pasteur, where I worked in the Manufacturing Technology department as a Study Lead. My projects focused on characterizing the manufacturing process for Bordetella pertussis antigens that Sanofi will generate in their new vaccine manufacturing facility.

I have also contributed to the drug discovery process at both Zymeworks Inc. and Phenomic AI, two biotech companies in Canada that are working to develop the next big cancer therapeutic. In my current role on the Protein Science team at Phenomic, I carry out the expression, purification, and characterization of proteins of interest so that they can be evaluated as potential therapeutics.

Hello! I did my PhD studies in the Davies lab from 2010-2015, studying antifreeze protein structure and function. My primary research focus was a novel antifreeze protein from winter flounder. We called it “Maxi”. It was a challenging protein to work with since it is very thermolabile and had to be crystallized in the cold room. With the great support from Peter, Nelson, Rob. C., Sherry, and my other labmates, I eventually solved the crystal structure of “Maxi”. It was a four-helix bundle protein stabilized by ~400 internal waters, which we published in Science in 2014. After graduating from Queen's, I continued pursuing structural biology and joined Natalie Strynadka’s lab at UBC as a postdoc, where I had an opportunity to express and a purify membrane protein and solve its structure using cryo-EM. After my postdoc training, I decided to move to industry. Currently, I am a Scientist in the Protein Technology team at Amgen Canada in Burnaby, BC. My job focus is to design and produce protein targets for drug discovery. However, my biochemistry background in protein characterization and structural biology helps me to work effectively in a drug discovery team. I am very grateful to live in Vancouver with my wife and son and have a job that I am passionate about. 

Following completion of my PhD in Physics at Simon Fraser University, Burnaby Canada in 1983 plus some generous Molecular Biology mentoring from members of the Simon Fraser Biology Department I was extremely fortunate in 1984 to be offered a position in lab of Peter Davies where the preeminent issue was the cloning of the type I antifreeze protein (AFP) genes from the Winter Flounder.  These were truly exciting times as the amplified structure of the flounder’s antifreeze gene locus gave birth to the idea that AFP gene amplification was driven by the rapid cooling of the oceans induced by Cenozoic glaciation.  Resolving the evolutionary consequences of Cenozoic glaciation on AFP gene evolution remains an active area of research particularly in the Davies’ lab and while the temptation to remain with Peter was strong I did head west to San Francisco in 1986 to join a lab at UCSF studying breast cancer.  In 2000 our UCSF lab relocated to the Buck Institute, a newly opened Institute in Marin County dedicated to the problems of aging.  Currently, as a Senior Scientist, my studies have explored various topics such as estrogen receptor activation and ERBB2 messenger RNA stability but the early days with Peter pondering Cenozoic glaciation and consequences for AFP gene evolution remains a career highlight.     

I did my PhD at Queen’s from 2015-2019. My projects were focused on developing microfluidic devices to study the microscale behavior of magnetotactic bacteria, oil-degrading bacteria, and bacteria with ice-binding protein, and their interaction with the surrounding environment. Working in Peter’s lab was an amazing and unforgettable experience.

In 2019, I joined Abbott Point of Care as Scientist. Since then, I have supported the development of a new immunoassay cartridge to measure cardiac troponin I (cTnI), which significantly improves the diagnosis and treatment of heart attack (myocardial infarction) at the early stages. I am passionate about working on innovative technologies that can advance human health, and help people live longer and better.

Apart from the technical skills needed to excel in such projects that are heavily multidisciplinary, I found that serving as a TA and mentoring students for their thesis projects during my MSc and PhD studies helped me a lot in successfully managing responsibilities in my current role. So, any experience and skill you gain might come in handy at some point.

I am blessed to have a wonderful wife and son, which make me the happiest man – at least in our home.

Salut! I did my PhD in Peter’s lab between 1996 and 2001 where we mapped the ice binding face of type I and type III antifreeze proteins using structure – function analysis.  I did my undergraduate and MSc at Simon Fraser University, after which I packed up my small Civic and drove across Canada to join the lab upon a recommendation of a friend who did his undergraduate in Biochemistry at Queen’s.  Kingston is a great place to go to school, there is lots to do and I met many people within the program and on campus who I will be friends with for life. I am a bit of a music nerd, so it was a gas to be able to have my own campus radio show for many years.  I also played on the Biochemistry department softball team, and met my future wife on a competing team, so you never know where things will take you!  I had a good foundation in all things biochemistry from my work in the group, so it wasn’t a stretch to go from antifreeze proteins to yeast protease expression systems as a post-doc at the NRC in Montreal.  I was fortunate to be able to become a Research Officer here.  I currently aid a lot of Canadian and international biotechnology companies with analytical assessment of their therapeutic candidates, and I work with the Molecular Modelling team and Mouse Monoclonal team at the NRC Montreal for the development, testing and screening of biotherapeutic candidates internally. The last few years have been all things COVID in conjunction with the new GMP plant at the Montreal site, now assessment of the quality attributes of spike protein and COVID therapeutics is currently a top priority. The job description is always shifting with the type of work that comes to us, so it is always interesting and new!

Hello! I first started in Peter’s lab in 2003 as a fourth-year thesis project student, and continued on as a PhD student from 2004-2010 studying the enzyme calpain and its inhibitor calpastatin. I really enjoyed protein structure-function studies and protein preps! My big breakthrough was co-crystallizing calpain-2 with a calpastatin inhibitory domain bound to it. This gave us the calcium-activated structure of calpain and its mechanism of inhibition by calpastatin, which we published in a 2008 Nature paper. After completing my thesis, I pursued protein structure-function studies as a PDF at the University of Toronto on phage-display used for antibody engineering. From there I worked as a Research Associate at The Hospital for Sick Children before joining Health Canada as a Biologist/Evaluator. Now, I work in the Biologic and Radiopharmaceutical Drugs Directorate, which regulates biological drugs, vaccines, radiopharmaceuticals, cells, tissues, and organs for human use. I evaluate the chemistry and manufacturing data for biologic drugs - no protein structure function studies and protein preps! I live in Ottawa with my family, and I am very appreciative of all the outdoor toddler-friendly activities Ottawa has to offer.

Early on in my PhD (’83-’89) I knew I wanted to become a ‘genetic engineer’. I followed with interest the early efforts of the Davies, Fletcher and Hew labs in making freeze-resistant transgenic Atlantic salmon using a flounder antifreeze protein gene. My project involved expressing flounder and wolffish AFP genes in Drosophila melanogaster as a model system and was jointly supervised by Virginia Walker in the Department of Biology (My wife, Sue, was Virginia’s first PhD student. Married for 38.5 years, both of our daughters and our first grandson live in Nova Scotia). After postdoc training in Mario Capecchi’s lab, I established the University of Calgary’s Genome Engineering Facility. My team originally used embryonic stem cells (ESCs) as a conduit to generate genetically engineered mouse models. That experience also led us to deriving human embryonic stem cells and induced pluripotent stem cells. About 10 years ago, we pivoted to CRISPR and have extended our genetic engineering to human cell lines, to rats, and, in the near future, to pigs.    

Hello! I was a grad student at Queen’s from 1988 to 1995, initially an M.Sc. candidate then transferred to Ph.D. studies. I had the benefit of TWO great supervisors - Peter and Virginia Walker - for my project, optimizing transgenic expression of fish antifreeze protein, using Drosophila as a model organism (try explaining that to non-scientists!). I then moved to Lausanne for a Postdoc with Susan Gasser at the Swiss Institute for Experimental Cancer Research, using budding yeast to study the molecular mechanisms regulating the initiation of DNA replication. Much skiing, chocolate, cheese and data later I returned to Canada in 2000 to start up my own group in the Department of Biology at the University of Waterloo, continuing with yeast studies of DNA replication, and cell cycle checkpoints – with a few rainbow trout checkpoint protein investigations for good measure! In recent years I’ve taken on some administrative roles at UW, serving as Associate Dean of Science for Research (2013-18), and currently as Associate Vice-President, Interdisciplinary Research. Along the way, I have also become an avid runner … highly recommended to destress after a challenging day and a great way to experience new locales when travelling!

I was a graduate student in the Davies lab from 1985 to ‘91. Before joining the lab, I thought that I would like to pursue mechanisms controlling gene expression for my PhD, but then I met Peter and his very cool fish antifreeze proteins. I rapidly became enthralled by protein structure / function and spent the next six years working on production of these proteins using recombinant E. coli and transgenic drosophila. These were fun-filled years both in and out of the lab, and I remember fondly the camaraderie we all felt. This was the beginning of my career trajectory in protein engineering and after taking a four-month break to backpack through Europe and the Middle East, I did a post-doctoral fellowship with Heinrich Roder at Fox Chase Cancer Center in Philadelphia. This was a happy union of my skillset in recombinant DNA methods with their expertise in studying protein structure and folding by 2D-NMR. From there I joined a team developing recombinant subunit vaccines for Dengue Fever at Hawai’i Biotech, Inc in Honolulu. My wife and I thoroughly enjoyed living ‘island style’ for the next six years, and it was an exciting time professionally as well, as I received NIH funding for a pair of SBIR grants to make novel binding-proteins via combinatorial engineering of an (a/b)8-barrel protein framework. We moved from Hawai’i to Montana in the fall of ’99 and then on to Idaho the following year.  During that time, I received two more SBIR grants under the auspices of NovaPro Inc., a start-up biotech company I founded. Since transferring operations to Florida in 2005, NovaPro has grown to a privately funded biotech focused on using our platform technology to develop a smart phone-based device for early detection of cancer biomarkers as well as environmental contaminants and pathogens. Moreover, I feel particularly blessed to have had the flexibility afforded by my self-employment, to devote time to raising and enjoying our two children, now in university themselves.

Hi there! I did my PhD in Peter's lab from 2008-2014 where I worked on calpain and structure-based inhibitor design. After graduate studies, I did my first post-doctoral fellowship at SickKids hospital in Toronto with Dr. Lynne Howell. Applying my enzymology and protein biochemistry background to bacterial exopolysaccharide biosynthesis, I started to make a move into the field of carboyhydrate-active enzymes. And finally I ended up in Dr. Wade Abbott's lab at Agriculture and Agri-Food Canada doing a second post-doc and now settling in as a permanent senior technician with my own research projects. I currently work on the enzyme-mediated breakdown of carbohydrates within the gut, both during digestion of food or invasion of pathogens. Thanks to guidance from Peter and Rob C., I knew I loved doing research (and loved being the one to do it!). My past set me up well to be an enzymologist and protein biochemist with my hands in many different projects within the lab, and I get to mentor plenty of students in the group as well. I wouldn't be where I am today without the memories made during my PhD; long-term friendships forged in graduate school, the "Box of Feelings" ("excitapointed" anyone?), and Friday evenings at the Grad Club. It's a pretty good life to have ended up doing some really cool science with a view of the Rockies and the Badlands all from my office window, and get to explore them in my off-hours too!

Hello!  I did my PhD from 2005 to 2011 in Peter's lab, focusing on antifreeze protein structure and function.   Later I did my PDF in Cancer Drug Discovery at Princess Margaret Hospital.  Soon after, I joined Sanofi as a project manager, managing validation studies.  With an unexpected opportunity, I became a Quality System investigator for vaccine manufacturing and lab equipment.  Combining my scientific understanding with the engineering experience, I moved to a management role leading the calibration program for the vaccine site.  Subsequently, I joined the new manufacturing facility project to build a program for the equipment calibration and master data management.  In 2020, I joined the global business process development team to build an integrated maintenance program and enterprise resource planning (ERP) software. Now, I work as the subject matter expert, implementing the maintenance program across the globe.

Looking back, my PhD was absolutely an intriguing adventure with my amusing colleagues, and somehow got myself a wife out of it. 

[Peter's note: What Nels meant to say is that he met his lovely wife in our lab, and got himself a PhD out of it as well.]

Hello! I did my MSc in the Davies lab from 2000-2002 studying the Ca2+ dependence of calpain-3 (p94) that had been linked to muscular dystrophy. It was exciting to start my academic career at Queen’s with Dr. Davies (who preferred to be called Peter) as it set me up for the career I have today. Following my MSc I completed my PhD in Medical Genetics at Queen’s favourite rival, the University of Toronto, and then pursued further training in clinical epidemiology. I have since spent my career as a champion of evidence-based, data-driven policy and practice with several leadership roles in the healthcare system and hospitals including Cancer Care Ontario (CCO). There I provided strategic leadership for the evaluation, analytics, and quality improvement teams, with oversight for the quality management of the provincial cancer screening programs. Prior to joining CCO, I was the Senior Manager, Performance Improvement at the Centre for Addictions and Mental Health (CAMH), and Associate Director of Evidence and Guideline Development at the Registered Nurses’ Association of Ontario (RNAO) where I had the opportunity to lead development of RNAO’s first patient and public engagement strategy and council. I enjoyed a return to pure research as Research Director at the Richard Ivey International Centre for Health Innovation at Western University where I oversaw several research health innovation projects. I was fortunate to begin my career in healthcare at Health Quality Ontario where I grew with the organization as Director, Performance Measurement & Reporting and led the development of online reporting tools for long-term care, home care, hospital patient safety, and the development of Ontario’s first Primary Care Performance Measurement Framework. Today I live in Vaughan (GTA) with my husband and daughter, a social services worker, who runs the child & youth programming at a downtown community centre.

[Peter’s note: Michelle and I both grew up in Liverpool, UK].

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I was an MSc student in the lab from May 1990 – September 1992. My project, co-supervised by Virginia Walker, involved the expression of sea raven Type II anti-freeze protein in Drosophila melanogaster. Having grown up in a small rural community, I was excited to get a job as a lab technician at Agriculture & Agri-Food Canada on the Experimental Farm in Ottawa, where I could marry my interest in agriculture and molecular biology. I have worked with four different scientists during my 30 years there. The research  that I have been involved with ranges from the study of insect resistance in transgenic plants to the use of yeast as a model system for the elucidation of protein  targets of fungal mycotoxins to the study of metabolomics of plant pathogenic fungi. I have also greatly enjoyed supervising/mentoring many undergraduate, graduate and co-op students over the years. Working in the government has also afforded me a good work-life balance which has included the usual year-long parental leaves, as well as the ability to take un-paid leave during the summer months while raising young children. I also enjoy volunteering on various committees at work such as the social committee where I organized BBQ’s for the 250 staff and students, as well as a career development committee which was established to help younger technicians grow and progress in their career in government. In my spare time, I enjoy gardening, reading, running, (after doing a few 5K’s with my kids, I ran my first 10K in 2019!) and doing some volunteer work in my community. 

I have always felt grateful to have gotten wonderful training and life-advice from the Davies lab. And I have felt so lucky to have an interesting and challenging job where I get to work with equally passionate and dedicated people!

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Hi! I was in the Davies lab from 2002-2007, working on calpain family of proteases. I recall many team building, opportunities to travel to conferences (Arizona) or collaboration (Stanford U.), all with the support of a family-like team back in the lab.

After my Ph.D., I did a short post-doc at U of T, followed by 4 years at Cytochroma, a Queen’s University spin-off, working on development of Vitamin D-based drugs. (I take a small handful of vitamin D supplements every day to this day … and so should you!)

Since 2011 I have been at Sanofi Pasteur in Toronto, a site of >1500 people dedicated to vaccine manufacturing. I lead a team developing the framework, tools to improve our understanding of our antigen manufacturing processes to allow us to more easily modernize and innovate, while keeping inline with regulations (“Quality by Design” is the industry term for these concept).

Biologicals (pharmaceutical products of biological nature) have a strong potential in helping humanity. My experience with Peter and his team was invaluable in getting the foundation of how to study them, and a vision for an ideal working team culture. I have such fond memories of my years there.

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I was in Peter’s lab as PhD student in 1997-2002. Peter asked me “do you want the red pill or the blue pill?” I took the blue and what a ride it was working on the calpains at the turn of the century. Back then things were just taking off in structural biology, with the first crystallographer hired at Queen’s, Dr. Jia, who had recruited amazing talent including Chris, Dan, and Ante. We worked closely with Dr. Elce, Dr. Jia and their labs to crack how calpains were activated by calcium. Time in Peter’s lab was most definitely some of the best I’ve had in my life with a mix of hard work and lots of fun. The best part about it though is that I made some of my best friends while in Peter’s lab. After graduation, I joined Kalle Gehring’s lab at McGill in 2003-2006 as a postdoc and pursued a new line of research investigating the apoptotic BCL-2 proteins combining crystallography and NMR. I moved to St. Jude in 2006 to pursue another postdoc with Doug Green, who is known among others as Dr. MOMP (for mitochondrial outer membrane permeabilization which is regulated by the BCL-2 proteins). I ended up spending a few extra years with his team before I secured a PI position at St. Jude, first as Research Associate and now as Assistant Member. In my lab we study several forms of cell death combining structural and chemical biology. In Memphis, I met Susanna and we have two lovely kids, Grace (7) and Jack (3), which has made everything much better although now we have no time for much else besides work and having fun with the kids. If I were to do it over, I would not change a thing about starting my career in Peter’s lab! Peter is one of the best mentors I know. I often think about what Peter would do when I try to stir my trainees. Thank you, Peter, et al., miss you guys!

Welcome! I did my undergraduate and master’s degree in Pharmacy in India and then worked as a Research Scientist at Ranbaxy Laboratories within their new-drug discovery research division. Following this industrial career, I moved to Saskatoon in December 2005 (from +25 °C to -25 °C) to purse a PhD in Chemistry at the University of Saskatchewan under the guidance Professor David Sanders. Following my PhD, I had the opportunity to join Peter’s lab as a postdoctoral fellow in 2010 to work on calpain structure-function and also develop small molecule inhibitors of calpain. As a mentor, Peter gave me an excellent opportunity to pursue my interests on fragment-based drug discovery for calpain that eventually led to collaborative work with Structural Genomics Consortium at Toronto. Furthermore, I had the opportunity to do structural studies on Calpain-3 that led to the structure determination of its PEF domain that makes this enzyme form a homodimer. Peter’s lab provided me an opportunity to train or assist other graduate students in the lab especially in protein crystallization and crystallography. In 2013, I moved to University of Calgary as Eyes High Postdoctoral fellow to purse a research program on iron-binding proteins that are essential for certain pathogenic bacteria. After a brief stay at Calgary, I decided to move to the States and had a great opportunity at Stanford University to work with Ted Jardetzky, Department of Structural Biology. At Stanford, I learned a wide range of biophysical techniques (e.g., SPR) and used them for some ground-breaking small molecule discovery research. In 2017, I joined Abbvie (Chicago area) as a Senior Scientist in the biophysics team to provide expertise in a wide range of biophysical binding studies for various early drug discovery programs.

I was one of Peter’s first graduate students and completed my M.Sc. and Ph.D. at Queen’s, studying chromatin structure and transcription during spermatogenesis in the winter flounder (1979 – 1984). I continued in the Davies’ lab after my Ph.D. working with Peter to clone the rat cardionatrin (atrial natriuretic factor) cDNA. The cardionatrin project was a fun experience since we were competing against much larger labs with significantly more resources, but nevertheless, we were successful in being one the first labs to publish the cDNA sequence. In 1989, after my post-doctoral studies with Jim McGhee in Calgary studying gut tissue development in C. elegans, I accepted a Senior Scientist position (molecular biology) with Merck Frosst research laboratories (MRL) in Montreal. My career in drug discovery with Merck initially focused on drug targets within the Arachidonic Acid Cascade where we developed a novel PPAR assay that was used in the development of the leukotriene antagonist, Singulair, a novel and successful treatment for asthma sufferers. My team led the biology efforts for the PLA2 program and initiated the cyclooxygenase-2 project where we obtained the patent for the human Cox-2 cDNA and identified the key assays that lead to the development of the Cox-2 inhibitors Vioxx and Arcoxia; these were the first non-steroidal anti-inflammatories that targeted Cox-2 with the added benefit of stomach sparing. My group then established the Metabolic Disorders drug discovery efforts at Merck Frosst where we were the first to demonstrate, using mouse knockout studies that PTP-1B was the negative regulator of insulin signalling. In addition, to PTP-1B, my group was responsible for several diabetes and obesity drug discovery programs and implemented some early animal studies that eventually led to the development of the DPP-4 inhibitor Januvia, a novel first in its class for the treatment of diabetes. 

Merck decided to close the Merck Frosst laboratories in 2010. Rather than relocate to the USA, two colleagues and I started Kaneq Pharma to develop the PTP-1B inhibitor KQ-791 for the treatment of type 2 diabetes. We were successful in getting this into clinical trials, but unfortunately saw no significant effect at the doses used. Since 2016, my wife and I have retired to a lake-side property where we fish, cross-country ski, snowmobile and enjoy building children’s furniture for our first grandchild.

During my MSc and PhD studies in the Davies lab I transformed antifreeze protein genes into tobacco plants as a bioreactor model for molecular farming of proteins. Following graduate school, I was a post-doctoral fellow at Agriculture and Agri-Food Canada in London Ontario and then a research scientist at the Alberta Research Council (Vegreville). My focus broadened from molecular farming to more general molecular biology use across agriculture. In my current position as R&D Manager for a commercial seed testing company, I develop and validate molecular-based diagnostics for use in ensuring quality seed. The challenge of what I do is to trawl through published work finding suitable resources or protocols that can be adapted to work for different domestic and international trade needs. We also work with multiple sample matrices including seed, soil, plant, fungi, and bacteria. Our test portfolio now encompasses: species identification in support of pathogen and seed purity regulation; pathotyping for effective seed variety selection; varietal identity checks for certified seed-use and supporting Canada’s end-use quality class system for cereals; refuge quantitation in insect-resistant varietal blends; and GM testing for hybrid production, varietal registration, intellectual property protection, and adventitious presence. Three of our pathogen tests have won awards as industry innovations.

It is deeply satisfying to see the results of your work be used in real time. l also value the range of perspectives I encounter throughout the industry with clients, commodity groups, researchers, regulators, and my colleagues on international committees for molecular diagnostics in agriculture. It is amusingly ironic that at one of our last pre-COVID meetings, part of the discussion was developing a standard method for detection of transgenic fish with enhanced growth capability—a project I remember well from the Davies lab collaborations with U of T and Memorial University. Put me in, Coach, I have absolutely got this!

Greetings from Singapore! I did my PhD in the Davies lab from 1995 to 2000. At our first meeting, Peter offered me four projects, sketched by pencil, including three on fish antifreeze proteins (AFP) and one on a new insect AFP. It was a difficult decision because all projects sounded exciting. I finally decided to work on the insect AFP because my wife did not eat fish J. Looking back, I consider myself lucky to help start up the exciting era of the new hyperactive insect AFPs. I still recalled the joyful moments of seeing the TmAFP repetitive sequence and solving the beautiful beta-helical protein structure. It was not an easy project; lots of difficulties from cloning, expression, refolding, and solving the structures. A great project will not work out without guidance from a wise supervisor and many stimulating beer-discussions with a group of clever labmates (Sherry, Laurie, Carl, Michele, Jason, Tudors, Chris(s)…) plus my own some crazy ideas (ie. double cream, single sugar; 4 °C wine-fermenting AFP, etc.). Apart from research, I had so much fun time and friendship in the lab, playing softball, goldfish, winter bugs searching, synchrotron trip, Peter’s red canoe, BBQ at Peter’s backyard, as well as the 1998 ice storm…etc.  The PhD time in the Peter’s lab was really one of the best time that I have had in my life. After graduation from Queen’s, I joined Kun Ping Lu’s lab, as a post-doc, at the Harvard Medical School in 2000-2003, working on the roles of the peptidyl cis/trans isomerase Pin1 in human diseases such as cancer and Alzheimer disease. In 2003, I moved to the National University of Singapore and established my own lab here. We are working on understanding fundamental aspects of chromosome oscillation mediated by microtubules, and mitochondrial dynamics and quality control.  In addition to my research and teaching, I have been in several administrative positions serving as Deputy Head of the Department, for graduate matters and research, and the Director for the Special Program in Science at NUS. Occasionally I escape from these heavy duties and enjoy mountain trekking. My wife and I have been to EBC and APC in Nepal and some nice trails in China. You are welcome to visit us in Singapore!!  

I’m Cathy Watson and I was in Peter’s lab from 1990-95. I didn’t work on anti-freeze, but instead investigated the genetic and protein structure of highly repetitive sperm proteins of winter flounder. After getting my PhD, I did a couple of postdocs where I continued to investigate gene regulation, but in human diseases (cancer and heart disease). Life took me to Ann Arbor, MI where I landed a position as a liaison between a startup biotech company and their collaborator at the University of Michigan.  My willingness to help out with many different types of activities allowed me to get a broad experience in drug development, and I realized that I really enjoyed clinical trials.  My ability to understand scientific concepts quickly teamed with my organizational and technical writing skills were highly marketable, and I took a position at Novartis Pharmaceuticals in what would become their Translational Medicine department.  I loved this niche of clinical development where we took new drugs from the basic scientists and tested them for the first time in humans.  I stayed with Novartis for 14 years, then retired to spend summers in Maine and winters in BC.

Hi, I’m Emily. I completed my MSc in the Davies lab by researching the evolution of type II antifreeze proteins in fish. During my time at Queen's, I worked for the Canadian Science Fair Journal and as a Spotlight Writer for the School of Graduate Studies. I also volunteered as the MC and Sponsorship Coordinator for the regional science fair and served as Marketing Director of the Science to Business Network (Kingston Chapter). I leveraged my thesis and extracurricular experience to start working as a Medical Communications Writer for a life science consulting firm (Sixsense Strategy Group), and also continue to work as the Managing Editor of the CSFJ. You can find me at https://www.linkedin.com/in/emily-lind/.

Hello there! I first started in Peter’s lab in 2019 as a fourth-year thesis project student and continued as a MSc student from 2020-2022. My project focused on functionally characterizing the RTX adhesin of a pathogenic bacterium called Vibrio cholerae. By understanding the biological role of the adhesin, we will be able to identify inhibitors to block attachment to host cells. In my unbiased opinion, I had the most interesting project (shhhh don’t tell Thomas, Mathias, or Rob).

During my 3 years with Peter, I learned a great deal about protein sciences and basic research. My thesis project involved molecular cloning, recombinant protein purification, ligand-binding studies, fluorescence microscopy, and many other exciting biochemistry techniques. With the training I got from Peter, Laurie, Qilu, Rob, and my other fellow lab mates, I am confident in my ability as a biochemist.

Currently, I am working as a Process Development Engineer at Regeneron, a large biotechnology company in New York, USA. My role requires me to optimize protein purification processes to maximize protein yield, purity, and stability. For my role, more than 200 unique proteins (e.g. mAbs, BsAbs, his-tagged, and alternative format antibodies) are purified a year. As you can imagine, having a strong foundation in protein biochemistry is important for designing purification strategies and analyzing data for the gazillions of proteins I encounter.

Peter is an exceptional mentor, not only in science, but also in life. Whenever I am faced with the dilemma of taking the elevator or stairs to reach upper floors in buildings, I always think to myself, “What would Peter do?” The answer is taking the stairs. I am grateful for the opportunities and experiences Peter has provided me. The Davies lab will always hold a special place in my heart.

Hello! I’m Mary. After graduating in Biochemistry at McGill I joined the Davies lab in summer 2020 for MSc research on bacterial adhesins. My research project covered some ‘environmental’ bacteria like those that colonize plant root surfaces and form beneficial biofilms. Their functions include promoting plant growth and preventing pathogenic fungal infection. I also studied the adhesin of an oil-degrading bacterium. AlphaFold2 arrived just in time to help sort out the structures of these huge proteins! I graduated this spring (2023) while working in Shanghai at AstraZeneca as a Drug Safety Associate. (I like their cafeteria and coffee bar!)  During my spare time, I enjoy music, films, watching soccer (Bayern Munich), and F1 racing.

Hello from Toronto! I started in Peter’s lab in 1999 as a M.Sc. student and finished a Ph.D. in 2005.  I graduated from Life Sciences at Queen’s in 1995, then spent some time working in industry and sailing to waters where fish don’t require antifreeze proteins. Before long, I felt drawn back to academia, Kingston and Queen’s, and found Peter’s research synopsis on antifreeze protein (AFP) structure, function and evolution very intriguing! Fortunately, he accepted me, and Sherry was there to teach me how to work in the lab. I began by characterizing a hyperactive AFP from the beetle Tenebrio molitor and performing some protein engineering to enhance its activity. We were tinkering with exploiting the binding of AFPs to ice to develop an affinity purification system, which led to the unexpected discovery of a hyperactive flounder AFP, which had been elusive because it is highly temperature sensitive.  The second part of my thesis was about characterizing this novel AFP. In my postdoc with Mitsu Ikura at Princess Margaret Cancer Centre in Toronto, I directed my interest in protein structure/function towards cancer signalling and the mechanisms of oncogenic mutations. I am particularly interested in the RAS family of small GTPase proteins, their regulators, and their effector proteins (e.g., MAPK and PI3K pathways). As a Staff Scientist at Princess Margaret, I am continuing related studies and managing facilities for ‘Protein Expression and Purification’ and ‘Biophysical Protein Characterization’. Thank you, Peter, for providing the supportive environment that brought me to the fascinating field of proteins!