Crystallographic Analysis of a Pepstatin Analogue Binding to the Aspartyl Proteinase Penicillopepsin at 1.8 Angstroms Resolution
Peptides: Structure and Function, Proceedings of the of the Eighth American Peptide Symposium (1983)
;Crystallographic Analysis of Transition State Mimics Bound to Penicillopepsin: Difluorostatine-and Difluorostatone-Containing Peptides
;
Biochemistry (1992)
Aspartic Proteinases and Their Catalytic Pathway
Biological Macromolecules and Assemblies (1987)
Stereochemical Analysis of Peptide Bond Hydrolysis Catalyzed by the Aspartic Proteinase Penicillopepsin
Biochemistry (1985)
X-Ray Diffraction Studies on Penicillopepsin and its Complexes: The Hydrolytic Mechanism
Aspartic Proteinases and Their Inhibitors (1985)
;Effect of Ph on the Activities of Penicillopepsin and Rhizopus Pepsin and a Proposal for the Productive Substrate Binding Mode in Penicillopepsin
;
Biochemistry (1984)
Structure and Refinement of Penicillopepsin at 1.8 Angstroms Resolution
J.Mol.Biol. (1983)
Conformational Flexibility in the Active Sites of Aspartyl Proteinases Revealed by a Pepstatin Fragment Binding to Penicillopepsin
Proc.Natl.Acad.Sci.USA (1982)
