Engineering fluorescent protein substrates for the AAA+ Lon protease
β Scribed by Wohlever, M. L.; Nager, A. R.; Baker, T. A.; Sauer, R. T.
- Book ID
- 118738763
- Publisher
- Oxford University Press
- Year
- 2013
- Tongue
- English
- Weight
- 330 KB
- Volume
- 26
- Category
- Article
- ISSN
- 1741-0126
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π SIMILAR VOLUMES
A continuous caseinolytic activity assay has been developed and characterized with trypsin, a serine protease, and transin, a metalloproteinase. Beta-casein labeled with both N-(7-dimethylamino-4-methylcoumarinyl)-maleimide (DACM) and fluorescein isothiocyanate (FITC) is used as the substrate in thi
the molecular mass of the labeled molecule, the greater BODIPY-a-casein is a new fluorescent protein subthe motion (rotation) will be and the lower the emitted strate designed for fluorescence polarization studies fluorescence polarization value. When a relatively large to measure proteolytic activi