hdl:10013/epic.31222
publisher:10.1016/j.micron.2003.10.017
Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin
Colangelo, N, Hellmann, N, Giomi, F, Bubacco, L, Di Muro, P, Salvato, B, Decker, H and Beltramini, M
;
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Folco.Giomi [ at ] awi.de
Abstract
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.
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Article
Authors
Colangelo, N, Hellmann, N, Giomi, F, Bubacco, L, Di Muro, P, Salvato, B, Decker, H and Beltramini, M
;
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Published
Eprint ID
19436
DOI
https://www.doi.org/10.1016/j.micron.2003.10.017
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Cite as
Colangelo, N.
,
Hellmann, N.
,
Giomi, F.
,
Bubacco, L.
,
Di Muro, P.
,
Salvato, B.
,
Decker, H.
and
Beltramini, M.
(2004):
Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin
,
Micron,
35
(1-2),
pp. 53-54
.
doi: https://www.doi.org/10.1016/j.micron.2003.10.017
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