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
X-ray, neutron and NMR studies of the catalytic mechanism of aspartic proteinases
✍ Scribed by Leighton Coates; Peter T. Erskine; Sanjay Mall; Raj Gill; Steve P. Wood; Dean A. A. Myles; Jonathan B. Cooper
- Book ID
- 105946225
- Publisher
- Springer
- Year
- 2006
- Tongue
- English
- Weight
- 516 KB
- Volume
- 35
- Category
- Article
- ISSN
- 1432-1017
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract We report the X‐ray analysis at 2.0 Å resolution for crystals of the aspartic proteinase endothiapepsin (EC 3.4.23.6) complexed with a potent difluorostatone‐containing tripeptide renin inhibitor (CP‐81,282). The scissile bond surrogate, an electrophilic ketone, is hydrated in the compl
A conformational study of cycloveratrilenes 3 and 4 by high resolution NMR at low temperature for 3 and room temperature for 4 along with X-ray crystallography is reported. From these experiments we found a dynamic process, where magnetic and topologic environment are exchanged by conformational var