Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin.
Hemocyanin sequences allineament shows the presence of highly invariant regions especially in the active site and in the tight intersubunits interaction sites. Comparing the aminoacids in contact regions between monomers is possible to interpret the stability of hexamers.
Colangelo
N
N
Department of Biology, University of Padova, Via Ugo Bassi 58/B, Padova 35131, Italy.
Hellmann
N
N
Giomi
F
F
Bubacco
L
L
Di Muro
P
P
Salvato
B
B
Decker
H
H
Beltramini
M
M
D000818:Animals; D006433:Hemocyanins / Q000737:chemistry* / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism*; D033561:Penaeidae / Q000737:chemistry*; D011487:Protein Conformation
D006433:Hemocyanins; D010100:Oxygen