6533b826fe1ef96bd1285139
RESEARCH PRODUCT
Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin
Mariano BeltraminiNadja HellmannFolco GiomiNicholas ColangeloP. Di MuroBenedetto SalvatoHeinz DeckerLuigi Bubaccosubject
Protein Conformationmedicine.medical_treatmentGeneral Physics and AstronomyBiologyPenaeus monodon03 medical and health scienceschemistry.chemical_compound0302 clinical medicinePenaeidaeStructural BiologymedicineAnimalsGeneral Materials Science030304 developmental biology0303 health sciencesEcologyActive siteHemocyaninCell Biologybiology.organism_classificationOxygenMonomerchemistryHemocyaninsBiophysicsbiology.proteinProtein quaternary structureConformational stability030217 neurology & neurosurgeryOxygen bindingdescription
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.
year | journal | country | edition | language |
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2004-03-24 |