Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …

Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …

Zr (IV)-based metal–organic frameworks (MOFs) such as the Zr (IV) trimesate MOF-808 are
promising materials for catalytic applications. In this work, we report an aqueous solution …

Activation of metalloprodrugs or prodrug activation using transition metal catalysts
represents emerging strategies for drug development; however, they are frequently …

Today, proteins are typically overexpressed using solubility-enhancing fusion tags that allow
for affinity chromatographic purification and subsequent removal by site-specific protease …

Protein chemical synthesis offers useful and otherwise-difficulty-to-obtain
biomacromolecules for biological and pharmaceutical studies. Recently, the hydrazide …

Site-specific protein cleavage is essential for many protein-production protocols and
typically requires proteases. We report the development of a chemical protein-cleavage …

Schneidewerkzeug: Zn (OTf) 2 ist ein effizienter Katalysator für die selektive Spaltung von
Amiden mit β‐Hydroxyethylgruppe am Stickstoffatom. Der Mechanismus umfasst eine N, O …

Zinc finger proteins are abundant in the human proteome and are responsible for a variety of
functions. The domains that constitute zinc finger proteins are compact spherical structures …

Metal-assisted hydrolysis of peptide bond is a promising alternative for enzymatic cleavage
of proteins with prospective applications in biochemistry and bioengineering. Many metal …