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Circular dichroism studies on repeating polypeptide sequences of abductin
Author(s) -
Bochicchio Brigida,
Pepe Antonietta,
Tamburro Antonio M.
Publication year - 2005
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20172
Subject(s) - polyproline helix , chemistry , circular dichroism , chirality (physics) , protein secondary structure , stereochemistry , aqueous solution , elastin , solvent , crystallography , peptide , organic chemistry , biochemistry , medicine , chiral symmetry breaking , pathology , quantum mechanics , physics , nambu–jona lasinio model , quark
The secondary structure of abductin was investigated by CD and NMR studies of several synthetic peptides. Results obtained with these peptides showed the dominant conformations to be the polyproline II (PPII) structure in aqueous solution and different types of β‐turns in the less polar solvent trifluoroethanol. Accordingly, a preliminary structure–elasticity relationship for abductin, not unlike that currently accepted for elastin, is proposed. Chirality 17:364–372, 2005. © 2005 Wiley‐Liss, Inc.