Circular dichroism studies of relaxin and insulin peptide chains
β Scribed by DU, YU-CANG ;MINASIAN, ELIZABETH ;TREGEAR, G.W. ;LEACH, S.J.
- Book ID
- 115097877
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 610 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0367-8377
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## Abstract Circular dichroic studies of a desmosine crosslinked peptide reveal a hitherto undescribed elastin spectrum possessing a weak negative band at 230β235 nm, a weak positive band at 215 nm, and a maximum negative band at 190 nm. The spectrum is sensitive to both pH and temperature displayi
Boronic acid derivatives of good peptide substrates of the serine proteases cause slow-binding inhibition, manifested as biphasic binding (Kettner and Shenvi: J. Biol Chem. 259:15106-15114, 1984). These inhibitors are thought to act as reaction-intermediate analogs. Three peptide boronic acids--Ac-P