Download Aspartic Proteinases: Structure, Function, Biology, and by Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana PDF

By Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana Rao-Naik (auth.), Kenji Takahashi (eds.)

The fifth overseas convention on Aspartic Proteinases was once hung on September 19 via 24, 1993, at Naito Museum of Pharmaceutical technology and undefined, Kawashima­ cho, Gifu Prefecture, Japan, approximately 15 miles northwest of Nagoya urban. approximately a hundred scientists attended the convention, together with fifty two from 14 international locations outdoor Japan, and 32 papers have been provided through invited audio system, and fifty eight papers as posters. the aim of this convention was once to provide and speak about new info at the constitution, functionality, and biology, and similar subject matters, together with biomedical implications, of aspartic proteinases, and this ebook is a collec­ tion of approximately the entire papers awarded on the assembly. Aspartic proteinases belong to at least one of the 4 significant periods of proteinases, the others being serine, cysteine, and metalloproteinases, and are so referred to as on the grounds that they've got catalytic aspartic acid residues in universal of their lively websites. so much of them are optimally lively at acidic pH, consequently the long-used identify "acid proteinases," which, certainly, was once the most important name of the 1st convention of this sequence. even though, a few of them are lively at round impartial pH, indicating their physiological roles in a much broader diversity of pH than hitherto considered.

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Extra resources for Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications

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W. D. R. Davies, Binding ofa reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action, Proc. Natl. Acad. of Sci. 84:7009-7013 (1987). 4. C. R. Sielecki, K. H. Gelb, Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides, Biochem. 31:3872-3886 (1992). Aspartic Proteinase Structures 31 5. B. Veerapandian, J. Cooper, A. L. L. W. B. Damon, DJ. Hoover, Direct observation by X-ray analysis of the tetrahedral 'intermediate' of aspartic proteinases, Protein Science 1 :322-328 (1992).

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