Disulfide bonds play a pivotal role in the folding and stability of many bacterial proteins, influencing not only their tertiary structure but also their biological activity. In bacteria, the ...
This research proposal presents a comprehensive investigation into the structural and functional integrity of disulfide bonds within therapeutic proteins, emphasizing their critical role in ...
In a recent study posted to the bioRxiv* preprint server, researchers discovered that the spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is susceptible to cleavage at ...
Make room, disulfide crosslinks. There’s a new kind of crosslink in proteins. Instead of an S–S bridge connecting two cysteine residues, it consists of an N–O–S bridge between a lysine and a cysteine.
Certain types of peptides and microproteins for drug discovery research can be made more efficiently and quickly using a reaction solvent that helps mimic nature's way Cysteine is one of the many ...
Misfolded proteins can appear as small aggregates, soluble monomers, or large insoluble inclusion bodies. While the fundamental biophysical mechanisms that cause cytotoxicity are not fully understood, ...
A recent study published in Advanced Materials introduces a new approach in 3D bioprinting using a cysteine-modified hyaluronic acid (HA-Cys) bioink. This formulation is dynamically crosslinked ...
A new wave of antibody-targeted anticancer therapies is showing great clinical promise, with the potential to transform cancer treatment. These antibody-drug conjugates (ADCs) are multicomponent ...
Sometimes, life can be a real drag—especially if you’re a protein weighed down by unwanted baggage. Researchers have unveiled evidence that these ponderous proteins could be involved in a range of ...
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