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A Neutron Laue Diffraction Study of Endothiapepsin: Implications for the Aspartic Proteinase Mechanism †

✍ Scribed by Coates, L.; Erskine, P. T.; Wood, S. P.; Myles, D. A. A.; Cooper, J. B.


Book ID
127201099
Publisher
American Chemical Society
Year
2001
Tongue
English
Weight
605 KB
Volume
40
Category
Article
ISSN
0006-2960

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Catalytic mechanism of the aspartate pro
✍ Georgios Iliadis; Georg Zundel; Bogumil Brzezinski 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 208 KB

The following FTIR difference spectra were studied: (pepsin) minus (Asp 215 or Asp 32 modified pepsin), (pepsin / pepstatin) minus (the modified pepsin / pepstatin), (at 40ЊC incubated pepsin / substrate) minus (pepsin / substrate at 4ЊC), and (at 40ЊC incubated pepsin / substrate) minus (EPNP modif