## Abstract An increasing number of experimental and theoretical studies have demonstrated the importance of the 3~10~‐helix/α‐helix/coil equilibrium for the structure and folding of peptides and proteins. One way to perturb this equilibrium is to introduce side‐chain interactions that stabilize or
The role of α-, 310-, and π-helix in helix→coil transitions
✍ Scribed by Roger Armen; Darwin O.V. Alonso; Valerie Daggett
- Book ID
- 119824153
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2003
- Tongue
- English
- Weight
- 819 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0961-8368
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📜 SIMILAR VOLUMES
We have already shown by CD and NMR techniques that the terminally protected homo-octapeptides Z (and Ac)-[L-(aMe)Val] 8 -OtBu undergo a slow and irreversible 3 10 -helix to a-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under
## Abstract Monte‐Carlo calculations of geometric and thermodynamic characteristics of the α‐helix and the β‐structure of polypeptides have been carried out. To describe a hydrogen bond both the Lippincott–Schroeder and Morse potentials were used. The internal rotation angles φ and ψ in the α‐helix
The volume increment per amino acid residue for the a-helix to @-form transition of uncharged poly-clysine in aqueous solution was 3.8 ml in water and 4.3 ml in 0.2M and 1M NaBr solutions at 26"C, respectively. The sound velocity of the polymer solution was greater with the a-helix than with the @-f