Helix formation by hydroxyamyl-L-glutaminyl residues in water and aqueous sodium dodecyl sulfate
✍ Scribed by Trina Overgaard; Dorothy Erie; J. A. Darsey; Wayne L. Mattice
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1984
- Tongue
- English
- Weight
- 413 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Conformational properties of the hydroxyamyl-L-glutaminyl residue have been deduced from a CD study of two copolypeptides containing hydroxypropyl-L-glutaminyl residues. Mole fractions of hydroxyamyl-L-glutaminyl residues were 0.17 and 0.45. Zimm-Bragg statistical weights for the hydroxyamyl-L-glutaminyl residue in water are found to be similar to those determined by P.H. von Dreele, N. Lotan, V.S. Ananthanarayanan, R.H. Andreatta, D. Poland, and H.A. Scheraga [(1971) Macromolecules 4,40% 4171 for the hydroxybutyl-L-glutaminyl residue. Sodium dodecyl sulfate has only a marginal effect on the helix-forming tendency of hydroxyamyl-L-glutaminyl residues in water.