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.
Bochicchio
Brigida
B
Department of Chemistry, Università degli Studi della Basilicata, Potenza, Italy.
Pepe
Antonietta
A
Tamburro
Antonio M
AM
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