Circular dichroism studies on repeating polypeptide sequences of abductin.
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 beta-turns in the less polar solvent trifluoroethanol. Accordingly, a preliminary structure-elasticity relationship for abductin, not unlike that currently accepted for elastin, is proposed.
Department of Chemistry, Università degli Studi della Basilicata, Potenza, Italy.
Brigida
B
Bochicchio
Antonietta
A
Pepe
Antonio M
AM
Tamburro
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D046529:Microscopy, Electron, Transmission; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure
C023706:Abductin; D011506:Proteins