Penicillopepsin

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

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

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

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

Intrinsic spectral and kinetic properties of penicillopepsin and its action on N-acetylalanylalanyllysyl-p… (More)

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

Crystals of the molecular complex between the esterified tripeptide fragment of pepstatin and the aspartyl proteinase… (More)

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

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

The crystal structure of penicillopepsin, an extracellular acid protease isolated from the mold Penicillium janthinellum, has… (More)