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Vacuum‐ultraviolet circular dichroism of chondroitins and their complexes with poly( L ‐arginine)
Author(s) -
Stipanovic Arthur J.,
Stevens E. S.
Publication year - 1981
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.1981.360200713
Subject(s) - chemistry , circular dichroism , random coil , ultraviolet , crystallography , dichroic glass , helix (gastropod) , arginine , amino acid , optics , biochemistry , ecology , physics , snail , biology
The vacuum‐ultraviolet circular dichroism (VUCD) of chondroitin and chontroitin‐6‐sulfate has been measured to 160 nm for films and to 170 nm for D 2 O solutions. The pD‐dependent dichroic behavior of these glycosaminoglycans in D 2 O is similar above 200 nm and is in agreement with previous studies. Near 190 nm, the CD band sign is also dependent on pD. VUCD spectra were recorded for films and solutions of poly( L ‐arginine). In trifluoroethanol the polypeptide is α‐helical, while in D 2 O it exists as a random coil. The well‐characterized coil–helix transition of poly( L ‐arginine) during complexation with chondroitin‐6‐sulfate was observed by VUCD, including the previously inaccessible entire π → π* band. By construction of difference spectra it was also possible to monitor the VUCD of the polysaccharide component during complexation.