## Abstract This article measures the rates of folding and unfolding of the collagen‐like peptide (Pro‐Hyp‐Gly)~10~ over overlapping concentration and temperature ranges. The data allow calculation of the orders of the folding and the unfolding reactions, the effective Arrhenius activation energies
Potential energy surface and kinetics of the helix–coil transition in a 33-peptide
✍ Scribed by Giorgia Brancolini; Alessandro Venturini; Francesco Zerbetto
- Book ID
- 105886032
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 442 KB
- Volume
- 118
- Category
- Article
- ISSN
- 1432-2234
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📜 SIMILAR VOLUMES
A comparison has been made of the intrachain potential energy of an infinite straight a-helix of poly-L-alanine with that of the distorted form adopted in a coiled coil conformation. The energy terms included were the van der Waal's, electrostatic, hydrogen-bond, and the rotational potential terms.
## Values of the rue a~ which an alkrnaring copolymcric nucleic acid mclw ar~er a hzmpcn~urejump have been oblaincd wilh a Monle Carlo simulation. Using a Glauber-king scheme 10 model the dynamics. the helix-random coil transilion shows a pure "monodispersive" rslaxalion in accord with previous an