6533b83afe1ef96bd12a7b3d
RESEARCH PRODUCT
Extraordinary stability of hemocyanins from L. polyphemus and E. californicum studied using infrared spectroscopy from 294 to 20 K
Mireille KhalilZahia Boubegtiten-fezouaNadja HellmannPetra Hellwigsubject
0301 basic medicineSpectrophotometry InfraredÉlectrochimieInfraredAnalytical chemistryGeneral Physics and AstronomyInfrared spectroscopySpectroscopieCold treatmentProtein Structure SecondaryArthropod Proteins03 medical and health scienceschemistry.chemical_compoundHorseshoe CrabsAnimalsPhysical and Theoretical ChemistryProtein secondary structurebiologySpectroélectrochimieSpidersbiology.organism_classificationTemperature inducedChimie Physique[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallography030104 developmental biologyMyoglobinchemistryPolyphemusLimulusHemocyaninsdescription
International audience; Hemocyanins are large oligomeric respiratory proteins found in many arthropods and molluscs. Here we give infrared spectroscopic evidence of a high stability towards exposure to sub-zero temperatures for hemocyanins from the arthropods Limulus polyphemus and Eurypelma californicum at different pH values. Small but distinct temperature induced changes of the secondary structure were observed, but a stable core of at least 40% α-helical structure is preserved as identified in the infrared spectra obtained between 294 and 20 K. The structural changes differ in detail somewhat for the two hemocyanins, with overall fewer changes observed in the case of E. californicum. Notably, in both cases the overall changes in the α-helical content are found to be fully reversible. The small changes in the secondary structure and reversibility upon cold treatment seem to be a particular property of the two hemocyanins, since it was not observed for myoglobin studied in the same way.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2016-09-22 | Physical Chemistry Chemical Physics |