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Helix formation by hydroxyamyl‐ L ‐glutaminyl residues in water and aqueous sodium dodecyl sulfate
Author(s) -
Overgaard Trina,
Erie Dorothy,
Darsey J. A.,
Mattice Wayne L.
Publication year - 1984
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360230812
Subject(s) - chemistry , residue (chemistry) , sodium dodecyl sulfate , aqueous solution , sulfate , sodium , macromolecule , helix (gastropod) , chromatography , nuclear chemistry , organic chemistry , biochemistry , ecology , snail , biology
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.