## Abstract An __ab initio__ method has been developed to predict helix formation for polypeptides. The approach relies on the systematic analysis of overlapping oligopeptides to determine the helical propensity for individual residues. Detailed atomistic level modeling, including entropic contribu
Predicted and trifluoroethanol-induced α-helicity of polypeptides
✍ Scribed by Mary Koeppe Luidens; James Figge; Kimberly Breese; Sandor Vajda
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1998
- Tongue
- English
- Weight
- 801 KB
- Volume
- 39
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
The a-helix stabilizing solvent 2,2,2-trifluoroethanol (TFE) is.fiequently used as a medium for determining the average a-helicity of polypeptides by CD spectroscopy. CD spectra measured in solutions containing 10. 15, 20, SO, and 90% (vol/vol) TFE are presented,for S peptides that were selected to demonstrate possible variations in the effect of TFE concentration on the secondary structure. The analysis is extended to 6 further peptides whose CD spectra as measured in TFE are documented in the literature. The observed a-helicity at a high TFE concentration is compared with the a-helicity determined by a structure prediction method that combines conformational filtering [
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Absorption spectra and induced CD have been measured on aqueous solutions of watersoluble porphyrins with a-helical poly (L-glutamic acid) or a-helical poly (L-lysine) a t different mixing ratios. For the former, porphyrin is porphine-meso-tetra (4-N-methylpyridinium) (TMpyP) , and for the latter, i
## Abstract Vibrational CD (VCD) of amides A, I, and II vibrations of a variety of polypeptide films have been measured. VCD of films of α‐helical and β‐sheet structures are compared in the three regions. Reproducible spectra could only be obtained for thin films free of orientation dependence. The