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

Overgaard Trina | Zendy; Erie Dorothy | Zendy; Darsey J. A. | Zendy; Mattice Wayne L. | Zendy

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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.

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