Aspartic Proteinases: Structure, Function, Biology, and - download pdf or read online

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

ISBN-10: 1461357616

ISBN-13: 9781461357612

ISBN-10: 1461518717

ISBN-13: 9781461518716

The fifth foreign convention on Aspartic Proteinases used to be hung on September 19 via 24, 1993, at Naito Museum of Pharmaceutical technological know-how 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 nations outdoors Japan, and 32 papers have been offered by means of invited audio system, and fifty eight papers as posters. the aim of this convention was once to offer and talk about new info at the constitution, functionality, and biology, and comparable subject matters, together with biomedical implications, of aspartic proteinases, and this e-book is a collec­ tion of approximately the entire papers awarded on the assembly. Aspartic proteinases belong to 1 of the 4 significant periods of proteinases, the others being serine, cysteine, and metalloproteinases, and are so referred to as on account that they've got catalytic aspartic acid residues in universal of their energetic websites. so much of them are optimally lively at acidic pH, as a result the long-used identify "acid proteinases," which, certainly, was once the main name of the 1st convention of this sequence. besides the fact that, a few of them are energetic at round impartial pH, indicating their physiological roles in a much broader variety of pH than hitherto considered.

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

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B. Cooper, G. Khan, G. Taylor, U . L. Blundell, X-ray analysis of aspartic proteinases, ii. 3 A resolution, J. Mol. Bioi. 214: 199-222 (1990). 10. C. Abad-Zapatero, TJ. J. Neidhart, J. w. M. , Plenum Press, New York, London, 9-21 (1991). II. G. R. 8 A resolution, Nature (London) 319:33-35 (1986). 12. R. Sielecki, M. J. G. 8 A resolution, J. Mol. Bioi. 219:671-692 (1991). 13. A. Hartsuck, G. J. Remington, The high-resolution crystal structure of porcine pepsinogen, Proteins: Structure, Function and Genetics 13: 1-25 (1992).

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Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications by Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana Rao-Naik (auth.), Kenji Takahashi (eds.)


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