Intramolecular distortion of the α-helical structure of polypeptides
✍ Scribed by Yu.N. Chirgadze; E.V. Brazhnikov; N.A. Nevskaya
- Book ID
- 118917868
- Publisher
- Elsevier Science
- Year
- 1976
- Tongue
- English
- Weight
- 831 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A ngeles, Los A nge les, California 90024 ## Synopsis Solvent accessible peptide bonds in proteins exhibit a 1-3" compression of the OCN bond angle and a corresponding expansion of the NCCa bond angle, relative to buried peptide bonds. These changes are consistent with an increase in hydrogen bon
The a-helix stabilizing solvent 2,2,2-trifluoroethanol (TFE) is.fiequently used as a medium for determining the average a-helicity of polypeptides by CD spectroscopy. CD spectra measured in solutions containing 10. 15, 20, SO, and 90% (vol/vol) TFE are presented,for S peptides that were selected to