## 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 determination of the thermodynamic parameter of the helix-coil transition of polypeptides by means of dipole moment measurements
✍ Scribed by C. Dufour; E. Marchal
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1972
- Tongue
- English
- Weight
- 403 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The theoretical change of the mean‐square dipole moment of a polypeptide during the helix‐coil transition is compared with the change in helix content. It is shown that, according to the theory, the determination of the helix initiation parameter σ and the enthalpy of helix formation Δ__H__ can be determined. Experimental data on poly‐benzyl‐L‐gluatamate in two different solvent mixtures are given.
📜 SIMILAR VOLUMES
CQMMUNICATIONS TO THE EDITOR ## Conformation of Polypeptides i n the Helix-Coil Transition Region: Revised Calculation f o r the Fourth Moment Recently Birshtein' pointed out errors in our c.alc.ulation2 of the fourth monient (R4 ) We thus made revised calculations for (R4) and the deviation fro
## Abstract The approximations in the equation relating the viscosity of partially helical molecules to the cooperativity of the helix–random coil transition are investigated. Of the several approximations considered, only the neglect of long‐range intramolecular interactions in the random coil lea