Over the last decade, the ability to genetically encode unnatural amino acids (UAAs) has
evolved rapidly. The programmed incorporation of UAAs into recombinant proteins relies on …

Directed evolution circumvents our profound ignorance of how a protein's sequence
encodes its function by using iterative rounds of random mutation and artificial selection to …

Fluorinated analogues of the canonical α-L-amino acids have gained widespread attention
as building blocks that may endow peptides and proteins with advantageous biophysical …

INTRODUCTION Natural selection plays a central role in adaptive evolution, but we still
know little about its role in changing evolvability—the ability to bring forth new and adaptive …

Residue-specific incorporation of non-canonical amino acids into proteins allows facile
alteration and enhancement of protein properties. In this review, we describe recent …

Nature uses a limited set of metabolites to perform all of the biochemical reactions. To
increase the metabolic capabilities of biological systems, we have expanded the natural …

Developing technologies such as unnatural amino acid mutagenesis, non-natural cofactor
engineering, and computational design are generating proteins with novel functions; these …

Directed enzyme evolution has proven to be a powerful tool for improving a range of
properties of enzymes through consecutive rounds of diversification and selection. However …

The incorporation of noncanonical amino acids into proteins and protein-based materials
has significantly expanded the repertoire of available protein structures and chemistries …

Ryo Iizuka, Mai Yamagishi-Shirasaki, Takashi Funatsu. Green fluorescent protein (GFP) has
a chromophore that forms autocatalytically within the folded protein. Although many studies …