Conformational transitions of solubilized trout elastins
β Scribed by V. Guantieri; A. M. Jaques; A. Serafini-Fracassini; A. M. Tamburro
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1987
- Tongue
- English
- Weight
- 378 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ Synopsis
Synopsis
CD measurements on polypeptides obtained from trout elastin by mild acid hydrolysis (a-elastin) or cyanogen bromide cleavage (CB-elastin) are compared with the results of analogous studies on bovine a-elastin. The spectra show that bovine and trout elastin, despite their compositional differences, have a similar 8-turn content. This is discussed with reference to the molecular evolution of the protein and the function of 8-turns in elastin.
π SIMILAR VOLUMES
Conditions are described under which linear responses of optical density to time and enzyme concentration are experienced in the course of the elastase-catalyzed solubilization of remazol-brilliant-blue elastin. According to Gertler (1), elastase may be defined as a proteolytic enzyme which is able
Conformational studies on synthetic repetitive sequences and analogues of elastin are described. C D and nmr measurements gave evidence of flexible ,&turns as the dominant structural feature whose stability was found t o decrease by increasing the number of repetitivc units. The sequences comprised
## Abstract We used highβprecision density and ultrasonic velocity measurements to characterize the native (N), molten globule (MG), and unfolded (U) conformations of apomyoglobin. The molten globule states that were studied in this work include the MG~pH4~(NaCl) state observed at pH 4 and 20 m__M_
and Kates119] based on the deuterium isotopic perturbation effect. An additional factor that supports this conclusion can be found by analyzing further the CH stretching region. In the hypothetical classical 2-norbornyl cation, the hyperconjugative interaction of the C ( 3 j H bonds with the formall