## 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 transition between straight and coiled-coil configurations of the α-helix
✍ Scribed by Zubay, Geoffrey
- Book ID
- 122562379
- Publisher
- Elsevier Science
- Year
- 1959
- Tongue
- English
- Weight
- 154 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0022-2836
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## SYNOPSIS Circular dichroism (CD) experiments in the backbone (200-240 n m ) region are reported for four isolated, excised two-chain, coiled-coil segments whose chains comprise, respectively, residues 11-127,142-281,l-189, and 190-284 of the rabbit aa-tropomyosin ( T m ) sequence. The uv and CD
## Abstract The thermodynamics of the DNA helix‐coil transition is studied, starting from the thermodynamical potential difference between the states helix and coil; this potential difference is understood as the difference in free energies. With only three parameters obtained from experimental dat
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.