Trypsin has been used in a study to assess the ontogeny of the endocrine pancreas in the fetal/newborn baboon. Trypsin digestion and hydrogen/deuterium exchange support the transition between inward- and outward-facing conformations during the catalytic cycle of the bacterial multidrug ATP-binding cassette transporter.
A very active and very stable trypsin agarose derivative has been used to optimize the design of the synthesis of a model dipeptide, benzoylarginine leucinamide. Trypsin has also been used in a study to investigate protonation-state determination in proteins using high-resolution X-ray crystallography.
The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Lys-acetylated trypsin is less susceptible to autolysis than the native form.
