Latest News

GCE4All Receives NSF CFIRE Subaward

NSF's Initiative Advancing Cell-Free Systems Toward Increased Range of Use-Inspired Applications (CFIRE) invests more than $32M in biotechnology, accelerating the adoption of cell-free systems that will benefit multiple industries, including pharmaceuticals, biomanufacturing, bioelectrochemistry and agrochemicals

Oregon State University plays a central enabling role in the NSF CFIRE collaboration by supplying the core genetic code expansion technologies needed to build proteins with novel chemistries. The Mehl Lab and the GCE4All Center will provide engineered M. alvus orthogonal tRNA/synthetase pairs and specialized noncanonical amino acids that allow researchers to precisely label proteins, enhance their stability, engineer pi‑cation interactions, and replicate natural post‑translational modifications. These engineered components are uniquely powerful: they operate with high efficiency in all cell types, can be purified for seamless integration into cell‑free biosynthesis workflows, and can be stably encoded into B. subtilis for scalable production of designer proteins.

Through these contributions, OSU delivers the molecular toolkit that expands what proteins can do, adding to the team of experts assembled by Caravel for the CFIRE project.

Upcoming Talks on Genetic Code Expansion

Catch Ryan Mehl at one of these conferences to learn more about GCE4All work in person:

Featured Protocol of the Week by Nature

We are honored to have our latest publication featured as the protocol of the week of Sept 22, 2025! We hope you check it out!

Successful 2025 GCE Workshop

The 2025 GCE4All Center Workshop focused on the theory and practice of site-specifically installing non-canonical amino acids (ncAAs) that represent post-translational modifications (PTMs) in proteins. Academic and industrial attendees received hands-on training from Center scientists on how to express, purify, and characterize recombinant proteins containing site-specifically installed PTMs, including phospho-serine, non-hydrolyzable phospho-serine, phospho-threonine, acetyl-lysine, 3-nitro-tyrosine, and halogenated tyrosines. Academic attendees were invited to bring a gene of their choice for ncAA installation. A series of lectures discussed the practice, theory, history, strengths and challenges of Genetic Code Expansion as it relates to installing PTMs and characterizing PTM-proteins. This year's group of participants represented over 10 different academic and industry labs spanning 3 countries!

Nature Chemistry News & Views

Excited to see a DBP publication highlighted by Nature Chemistry, we hope it finds you NMR users!

"NMR spectroscopy is a critical tool for linking protein structure, dynamics and interactions to protein function, but is challenging to apply to high-molecular-weight proteins. The chemical synthesis of an NMR probe combines the advantages of four different nuclei, 1H, 2H, 13C and 19F, to achieve optimal resolution for these larger systems."