Penicillopepsin

The design of inhibitors with enhanced potency against proteolytic enzymes has many applications for the treatment of human… Expand

Solvation in macromolecular crystal structures was studied by analyzing X-ray diffraction data of two proteins, penicillopepsin… Expand

Analogies between the free R statistic [Brunger (1992). Nature (London), 355, 472–474] and the statistical methods of cross… Expand

Analogies between the free R statistic [Brünger (1992). Nature (London), 355, 472-474] and the statistical methods of cross… Expand

The molecular structures of three phosphorus-based peptide inhibitors of aspartyl proteinases complexed with penicillopepsin [1… Expand

The X-ray crystal structures of native penicillopepsin and of its complex with a synthetic analogue of the inhibitor pepstatin… Expand

Abstract Penicillopepsin, the aspartyl protease from the mould Penicillium janthinellum , has had its molecular structure refined… Expand

Crystals of the molecular complex between the esterified tripeptide fragment of pepstatin and the aspartyl proteinase… Expand

The polypeptide chain of the acid protease penicillopepsin folds via an 18-stranded mixed β-sheet into two distinct lobes… Expand

A proposed mechanism for the catalytic hydrolysis of peptide bonds by acid proteases is similar in many respects to the Zn… Expand