Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism.
The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a hydroxyproline-rich glycopeptide and its deglycosylated derivative. It is concluded that the lectin contains about 35% polyproline II conformation, 34% type II beta-turn and 31% irregular conformation. No indications were found for the presence of alpha-helix or beta-sheet conformations. The polyproline II conformation is heat-stable, but is markedly destabilized by deglycosylation. The type II beta-turn is destabilized by cleavage of disulphide bonds.
G J
GJ
van Holst
S R
SR
Martin
A K
AK
Allen
D
D
Ashford
N N
NN
Desai
A
A
Neuberger
D000596:Amino Acids / Q000032:analysis; D002241:Carbohydrates / Q000032:analysis; D002942:Circular Dichroism; D005561:Formates; D037102:Lectins; D010084:Oxidation-Reduction; D037121:Plant Lectins; D011487:Protein Conformation
D000596:Amino Acids; D002241:Carbohydrates; D005561:Formates; D037102:Lectins; D037121:Plant Lectins; C041202:potato lectin; C008817:peroxyformic acid