## Abstract Analogous with the Potts model that describes the helixโcoil transition in the isolated polypeptide chain (a Hamiltonian model allowing for the energy __U__ of hydrogen bond formation) the number Q of conformational states of a repeating unit of the chain and the topology of ฮ = 3 hydro
The helix-coil transition in polypeptides: A microscopic approach. II
โ Scribed by Sh. A. Hairyan; E. Sh. Mamasakhlisov; V. F. Morozov
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1995
- Tongue
- English
- Weight
- 610 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-3525
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๐ SIMILAR VOLUMES
## Abstract A simplified model of a polypeptide chain is described. Each residue is represented by a single interaction center. The energy of the chain and the force acting on each residue are given as a function of the residue coordinates. Terms to approximate the effect of solvent and the stabili
A simple way to incorporate the solvent-peptide interaction in any available theory of the helix-coil transition is developed. The competition between the intramolecular hydrogen bonding and the solvent-polymer hydrogen bonding is considered in multicomponent solvents where some of the components ha
## Conformation of Polypeptide i n the Helix-Coil Transition Region A recently published work by Go, Saito, and Ochiail presented a calculation of the mean values of the second (R2) and the fourth (R4) powers of the end-to-end distance of the polypeptide chain in the helix-coil transition region.
The helix-coil transitions for poly-L-lysine (PL) were investigated by the methods of spectropolarimetry, viscometry and potentiometric titration in 0.2M NaCl a t different temperatures as well as in 0.2M NaBr, 1M KC1, and in mixtures of 0.2M NaCl or NaBr with methanol a t room temperature. The enth