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Archives of Biochemistry and Biophysics

Volumn 439, Issue 1, 2005, Pages 42-52

Contribution of the copper ions in the dinuclear active site to the stability of Carcinus aestuarii hemocyanin

(6) Spinozzi, F a Gatto, S b De Filippis, V c Carsughi, F a Di Muro, P b Beltramini, M b

a UNIVERSITÀ POLITECNICA DELLE MARCHE (Italy)

b UNIVERSITY OF PADOVA (Italy)

c CRIBI Biotechnology Center (Italy)

Author keywords

CaeSS2 monomer; Circular dichroism; Copper; Hemocyanin; Limited proteolysis; Oligomerization; Small angle X ray scattering

Indexed keywords

COPPER ION; HEMOCYANIN; TRYPSIN;

ARTICLE; CARCINUS AESTUARII; CIRCULAR DICHROISM; CRUSTACEA; GEL FILTRATION CHROMATOGRAPHY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN STRUCTURE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ANIMALS; BINDING SITES; BRACHYURA; CIRCULAR DICHROISM; COPPER; HEMOCYANIN; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

CARCINUS AESTUARII;

EID: 20444461900 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/j.abb.2005.05.005 Document Type: Article

Times cited : (5)

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