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Circular dichroism studies of an elastin crosslinked peptide
Author(s) -
Foster J. A.,
Bruenger E.,
Rubin L.,
Imberman M.,
Kagan H.,
Mecham R.,
Franzblau C.
Publication year - 1976
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.1976.360150503
Subject(s) - elastin , chemistry , circular dichroism , peptide , peptide bond , desmosine , cleavage (geology) , crystallography , cotton effect , stereochemistry , biophysics , amino acid , biochemistry , materials science , medicine , pathology , fracture (geology) , composite material , biology
Circular dichroic studies of a desmosine crosslinked peptide reveal a hitherto undescribed elastin spectrum possessing a weak negative band at 230–235 nm, a weak positive band at 215 nm, and a maximum negative band at 190 nm. The spectrum is sensitive to both pH and temperature displaying increased ellipticity of the 215‐nm band at acidic pH and low temperature. The general shape of the spectrum and its behaviour toward temperature changes suggest the presence of an extended helical conformation. Susceptibility of insoluble elastin to digestion with chymotrypsin is increased tenfold at low temperature (4°C), supporting the contention that the conformational change of the type described above occurs in insoluble elastin. Such changes in conformation would result in increased availability of aromatic amino‐acid resiudues to peptide bond cleavage.