## 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
Helix–coil dynamics of a Z-helix hairpin
✍ Scribed by J. Antosiewicz; M. W. German; J. H. Van De Sande; D. Porschke
- Book ID
- 101718943
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1988
- Tongue
- English
- Weight
- 474 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Synopsis
The helix-coil transition of a Z-helix hairpin formed from d(C-G),T,(C-G), has been characterized by equilibrium melting and temperature jump experiments in 5M NaC10, and 10 mM Na,HPO,, pH 7.0. The melting curve can be represented by a simple all-or-none transition with a midpoint at 81.6 * 0.4OC and an enthalpy change of 287 k 15 kJ/mole. The temperature jump relaxation can be described by single exponentials at a reasonable accuracy. Amplitudes measured as a function of temperature provide equilibrium parameters consistent with those derived from equilibrium melting curves. The rate constants of Z-helix formation are found in the range from 1800 s-' a t 70°C to 800 s-' at 90°C and are assoCiated with an activation enthalpy of -(50 * 10) kJ/mole, whereas the rate constants of helix dissociation are found in the range from 200 s-' at 70°C to 4500 s-' at 90°C with an activation enthalpy +235 kJ/mole. These parameters are consistent with a requirement of 3-4 base pairs for helix nucleation. Apparently nucleation occurs in the Z-helix conformation, because a separate slow step corresonding to a B to Z transition has not been observed. In summary, the dynamics of the Z-helix-coil transition is very similar to that of previously investigated right-handed double helices.
📜 SIMILAR VOLUMES