Helix formation by hydroxyamyl‐ L ‐glutaminyl residues in water and aqueous sodium dodecyl sulfate

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. Ananthan‐arayanan, R.H. andreatta, D. Poland, and H.A. Scheraga [(1971) Macromolecules 4, 408–417] 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.