A carbodiimide-based condensing agent and additive improve solid-phase peptide conversion while preventing crystal precipitation.
A lysine-histidine acylation tag enables selective protein labeling without metal ions.
The process uses aqueous suspension and density separation to recover protein, non-gelatinized starch, and fiber without organic solvents.
This case combines liquid-phase synthesis, RP purification, lyophilization, and ion-pairing chromatography to control trace impurities.
Gradient-pH enzymatic hydrolysis modifies gliadin for uniform dispersion after heat sterilization, salt exposure, and storage.
A continuous flow-through sequence replaces Protein A chromatography with chelation, diafiltration, and orthogonal membrane adsorbers.
A non-covalent cucurbituril host holds two aryl guests, stabilizing biomolecules while enabling rapid release and simple filtration.
Visible-light LADA replaces unstable carbon-sulfur links with stable carbon-carbon bonds while preserving protein chirality.
Affinity, cation exchange, and mixed-mode chromatography reduce HMW aggregates by up to 95% and remove far-basic variants completely.
This case uses a solid-phase carrier, deprotection, condensation, and cyclization to simplify purification across peptide derivatives.
This case combines MacT, RD29B, and a 5'-UTR enhancer with p38 suppression in one vector to reduce culture time and cost.
A carboxylic acid derivative enables simple N-terminal amide bonding in natural proteins and peptides while reducing lysine side reactions.
Sulfite or bisulfite ions form a stable adduct that prevents dibenzofulvene regeneration and side reactions in peptide synthesis.
A mixed dispersion of protected amino acids, base, condensing agent, and water enables simpler peptide-bond formation with high purity.