## Abstract There have been many reports that the nuclear magnetic resonance (nmr) spectra of a large number of polypeptides exhibit peak doubling of the α‐carbon and the α‐carbon proton in the helix–coil transition region. One apparent exception to this generalization has been polypeptides with io
High-resolution study of the helix–coil transition of poly(L-glutamic acid): Spectroscopic data correlation and the discovery of a new transition
✍ Scribed by Hidechika Hayashi; Akiyoshi Wada
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 539 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
This article reports on both (1) the precision and capability of a computerized multidimensional spectrophotometric system recently developed in our laboratory and (2) the high‐resolution study of the helix–coil transition of poly(L‐glutamic acid)[poly(Glu)], especially with regard to the discovery of an overlooked transition which is attributable to order–disorder rearrangement of the poly(Glu) side chain in the α‐helical conformation. This study was made possible by the high performance of the system used. The simultaneous and continuous measurement of the circular dichroism, the absorbance and light‐scattering intensity, and the pH titration curve of poly(Glu) in aqueous salt solution was carried out under continuous scanning of pH ranging from 8 to 2. Besides the well‐known random coil to α‐helix transition that occurs at about pH 5.5, a highly cooperative transition, which is indicated as a small but definite step in several spectral dimensions, is observed for the first time at pH 4.3. The transition is ascribed to an order–disorder conversion of the side chain on the α‐helix backbone.
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