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Site-selective protein editing by backbone extension acyl rearrangements (Nat Chem Biol, 2025)

Researchers at the NSF Center for Genetically Encoded Materials (C-GEM) developed a novel and versatile chemo-ribosomal strategy to generate isolable quantities of protein-derived biopolymers containing site-specific backbone modifications. This strategy relies on an intramolecular backbone-extension acyl rearrangement (BEAR) reaction that post-translationally and site-specifically rearranges the… Read More »Site-selective protein editing by backbone extension acyl rearrangements (Nat Chem Biol, 2025)

High Yield, Low Magnesium Flexizyme Reactions in a Water-Ice Eutectic Phase (Biochemistry 2025)

By Joshua Davisson Better Flexizyme reactions! This paper describes a method to improve the yields of flexizyme-promoted tRNA aminoacylation in vitro. Inspired by possible origins of life reaction conditions, performing flexizyme reactions in an ice eutectic phase reduces some of the critical disadvantages of flexizyme… Read More »High Yield, Low Magnesium Flexizyme Reactions in a Water-Ice Eutectic Phase (Biochemistry 2025)

Professor Scott Miller Wins the ACS Gabor A. Somorjai Award for Creative Research in Catalysis

Congratulations to Scott Miller for winning the 2026 ACS Gabor A. Somorjai Award for Creative Research in Catalysis. This award recognizes outstanding theoretical, experimental, or developmental research resulting in the advancement of understanding or the application of catalysis. Miller is one of many ACS awardees… Read More »Professor Scott Miller Wins the ACS Gabor A. Somorjai Award for Creative Research in Catalysis

C-GEM renewed for Phase IIb

C-GEM has been renewed to continue solving chemistry’s “Holy Grail” problem of how to synthesize truly sequence-defined chemical polymers, oligomeric molecules possessing both a pre-determined, diverse sequence, and a defined length. In the last five years, C-GEM scientists have site-selectively generated C-C bonds in ribosomally… Read More »C-GEM renewed for Phase IIb

Structure of an archaeal ribosome reveals a divergent active site and hibernation factor (Nat Microbiol, 2025)

By Amos Nissley C-GEM researchers identified archaeal ribosomes with highly divergent peptidyl transferase centers (PTC). Cryo-EM structures of the Pyrobaculum calidifontis ribosome revealed that unique archaeal ribosomal protein (rProtein) sequences reorganize the PTC, enabling rRNA sequence variation. Modifying E. coli rProteins to resemble those in… Read More »Structure of an archaeal ribosome reveals a divergent active site and hibernation factor (Nat Microbiol, 2025)