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Conformational changes induced in ionized poly( L ‐arginine) and poly( L ‐histidine) by sodium dodecyl sulfate
Author(s) -
McCord Robert W.,
Blakeney Ernest W.,
Mattice Wayne L.
Publication year - 1977
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.1977.360160612
Subject(s) - chemistry , sodium dodecyl sulfate , circular dichroism , histidine , arginine , cationic polymerization , imidazole , aqueous solution , residue (chemistry) , sodium , crystallography , stereochemistry , amino acid , polymer chemistry , chromatography , organic chemistry , biochemistry
Circular dichroism spectra have been obtained for cationic poly( L ‐arginine) and poly( L ‐histidine) in aqueous solutions containing varying amounts of sodium dodecyl sulfate. The detergent induces a disorder‐order transition in both polypeptides. In each case the transition is cooperative and occurs when the ratio of detergent to amino acid residue is near unity. The ordered structure formed by poly( L ‐arginine) is readily identifiable as an α helix. Poly( L ‐histidine) appears to form a β structure in which the 211‐nm electronic absorption band of the imidazole group exhibits significant rotatory strength.