## 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.
On the double peak of NMR in the helix—coil transition region
✍ Scribed by Kuniaki Nagayama; Akiyoshi Wada
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1973
- Tongue
- English
- Weight
- 684 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
To attempt to resolve the controversy over “fast” and “slow” helix–coil transition rates in polypeptides, nuclear magnetic resonance spectra were measured for monodisperse poly‐γ‐benzyl‐L‐glutamate (PBLG). These results were compared with simulated line spectra which were computed by taking the molecular‐weight distribution into consideration. Broad but single peaks have been observed in 220 mHz nmr for the α‐CH and NH proton resonance spectra in the transition region. The shape of the line changes with the extent of polydispersity. Assuming a fast conversion rate, a molecular model of the helix–coil transition simulates these results. Consequently, the double peak which has been observed in the nmr of polypeptides at the helix–coil transition region is shown to result from the polydispersity in molecular weight.
📜 SIMILAR VOLUMES
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
a p a n synopsis Dielectric studies have been carried out for the helix-coil transition of poly-p-benzyl-Gaspartate with m-cresol as a solvent. The transition of the solute molecules has been sharply reflected as a characteristic change in the dielectric dispersion curves in changing temperature. Tw
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 double‐helical complex formed from m^6^m^9^A and poly U has been characterized by circular dichroism and u.v. spectrophotometry. The circular dichroism of the complex is similar to that of the double‐helical poly A poly U complex both in shape and in magnitude and thus indicates a q