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Effect of the Ph in the Conformation and Activity of the Acid Protease From Aspergillus saitoi

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The circular dichroism spectrum in the far UV-region (190-240 nm) indicates that the acid protease from Aspergillus saitoi contains appreciable amounts of beta-sheet. The structure-activity relationship of the protein is studied as a function of the pH.

Keywords: acid protease; aspergillus saitoi; cathepsins d e; gastricsin; pepsin; pepsinlilke acid proteases; renin

Document Type: Review Article


Publication date: April 1, 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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