Results 31 to 40 of about 71,291 (119)
Rational design of the genetic code expansion toolkit for in vivo encoding of D-amino acids
Once thought to be non-naturally occurring, D-amino acids (DAAs) have in recent years been revealed to play a wide range of physiological roles across the tree of life, including in human systems.
Han-Kai Jiang +15 more
doaj +1 more source
Selenocysteine, pyrrolysine and the unique energy metabolism of methanogenic archaea [PDF]
Methanogenic archaea are a group of strictly anaerobic microorganisms characterized by their strict dependence on the process of methanogenesis for energy conservation.
Rother, Michael +3 more
core +1 more source
Site‐Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids
Genetic code expansion (GCE) enables site‐specific installation of noncanonical amino acids containing bioorthogonal conjugation handles, allowing precise, homogeneous protein modification. This review examines the principles of orthogonal translation, surveys the chemistries available for chemoselective labeling, and highlights emerging multi‐site ...
Rahul Sarkar +2 more
wiley +2 more sources
Incorporation of Amino Acids with Long-Chain Terminal Olefins into Proteins
The increasing need for site-specific protein decorations that mimic natural posttranslational modifications requires access to a variety of noncanonical amino acids with moieties enabling bioorthogonal conjugation chemistry.
Matthias P. Exner +9 more
doaj +1 more source
In protein engineering and synthetic biology, Methanosarcina mazei pyrrolysyl-tRNA synthetase (MmPylRS), with its cognate tRNAPyl, is one of the most popular tools for site-specific incorporation of non-canonical amino acids (ncAAs).
Hsueh-Wei Tseng +5 more
doaj +1 more source
Coupling biosynthetic noncanonical amino acid production with genetic code expansion enables site‐specific incorporation of azatryptophans into PET‐degrading enzymes (PETases). By isosteric single‐atom editing of a conserved tryptophan, AzaPETases break the activity–stability trade‐off, delivering higher catalytic efficiency at elevated temperature and
Elwy H. Abdelkader +3 more
wiley +2 more sources
The incorporation of non-canonical amino acids (ncAAs) into ribosomally synthesized and post-translationally modified peptides, e.g., nisin from the Gram-positive bacterium Lactococcus lactis, bears great potential to expand the chemical space of various
Maike Bartholomae +6 more
doaj +1 more source
The ability to genetically encode non-natural amino acids (nnAAs) into proteins offers an expanded tool set for protein engineering. nnAAs containing unique functional moieties have enabled the study of post-translational modifications, protein ...
Gargi Roy +11 more
doaj +1 more source
Genetic encoding of noncanonical amino acids (ncAAs) through sense codon reassignment is an efficient tool for expanding the chemical functionality of proteins. Incorporation of multiple ncAAs, however, is particularly challenging.
Alessandro De Simone +3 more
doaj +1 more source
We report the discovery of a simple system through which variant pyrrolysyl-tRNA synthetase/tRNACUAPyl pairs created in Escherichia coli can be used to expand the genetic code of Saccharomyces cerevisiae.
Rajendra Uprety (1273764) +3 more
core +1 more source

