Christopher Frøhlich

@cfr016.bsky.social

Enzyme evolutionist at UiT- The Arctic University of Norwary

🧬 I'm looking for a Researcher (2 years) in Molecular Biology and Antimicrobial Resistance at UiT The ❄️Arctic University of Norway (Tromsø). 🔬 If you have experience building and screening enzyme libraries and characterising the variants that come out, get in touch.

Is it too early for a year review? 🤔 Research stays at ETH Zürich with Adrian Bunzel and at UBC Vancouver with Nobu 🤓. Now I’m moving labs to start as Associate Professor at UiT, which means organising freezer contents 📦. Two β-lactamase evolution preprints coming soon 🧬. Stay tuned!

📣 Preprint Alert: How can evolution recruit existing enzymes during bacterial lifestyle changes? Discover how mutations in a bifunctional enzyme 🔄 alter bacterial c-di-GMP metabolism, decoupling it from external polyamine signaling, and steering cells from a planktonic to a biofilm lifestyle 🦠

Biofilm selection constitutively activates c-di-GMP synthesis by the bifunctional enzyme MbaA

Biofilms, in which microbes are encased within a self-produced matrix, represent the primary mode of microbial life. Yet, our understanding of the molecular mechanisms governing biofilm formation rema...

biorxiv.org

Are you interested in how #epistasis shapes the AMR evolution? We showed that epistasis can be caused by independently modulating substrate binding and the chemical step ultimately changing the rate-limiting step in the catalytic cycle. @NatureCatalysis Full read: rdcu.be/dzqjk

Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase

Nature Catalysis - The reasons for epistasis, wherein mutations interact non-additively, are often not fully understood. Now it is found that shifting the rate-limiting step from substrate binding...

rdcu.be

Are you interested in how #epistasis shapes the AMR evolution? We showed that epistasis can be caused by independently modulating substrate binding and the chemical step ultimately changing the rate-limiting step in the catalytic cycle. @NatureCatalysis Full read: rdcu.be/dzqjk

Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase

Nature Catalysis - The reasons for epistasis, wherein mutations interact non-additively, are often not fully understood. Now it is found that shifting the rate-limiting step from substrate binding...

rdcu.be

🌟Exciting News! Our AMR & Biofilms research just received an 8M kroner grant from #HelseNord. Big thanks for supporting young researchers and fueling scientific innovation. Grateful to all who've contributed to this success. Looking forward to what comes next.