Proteins constitute the majority of nature's worker biomolecules. Designed for specific
functions, complex tertiary structures make proteins ideal candidates for analysing natural …

Chemical protein modification has emerged as an invaluable tool for the development of
modified proteins. The complementary use of both genetic and chemical methods has …

Nature endows life with a wide variety of sophisticated, synergistic, and highly functional
protein assemblies. Following Nature's inspiration to assemble protein building blocks into …

The late‐stage modification of structurally complex peptides bears great potential for drug
discovery, crop protection, and the pharmaceutical industry, among others. Whereas …

Post-translational modifications (PTMs) produce significant changes in the structural
properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes …

The modification of proteins with non‐protein entities is important for a wealth of
applications, and methods for chemically modifying proteins attract considerable attention …

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 …

The conjugation of biomolecules can impart materials with the bioactivity necessary to
modulate specific cell behaviors. While the biological roles of particular polypeptide …

Glycosylation is one of the most prevalent posttranslational modifications that profoundly
affects the structure and functions of proteins in a wide variety of biological recognition …

Abstract Manganese (I)‐catalyzed C− H alkynylations with organic halides occurred with
unparalleled substrate scope, and thus enabled step‐economical C− H functionalizations …