Solvent effects on the helix–coil transition in polypeptides
✍ Scribed by Mordechai Bixon; Shneior Lifson
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1966
- Tongue
- English
- Weight
- 359 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
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 have hydrogen-bonding capacity. Molecular averages are computed by using the theory of Lifson and Roig. The experimental data of Yang are analyzed, and the range of acceptable values of the equilibrium constants of hydrogen bond formation is deduced. The enthalpy of the transition in multicomponent solvents is calculated.
📜 SIMILAR VOLUMES
## 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 lattice model of Flory has been extended in order to consider equilibrium between isotropic and nematic phases containing helix-coil type chains. Nearly complete exclusion of coil sequences from the lyotropic nematic phase produces an enhanced cooperativity in the helixxoil transition. In poor s
The effects of deuteration and of changes in solvent composition on the thermodynamics of the helix-coil transition have been studied by calorimetric and optical measurements in the poly-7-benzyl-Lglutamatedichloroacetic acid-l,%dichloroethane system. For a given solvent composition, deuteration of