6533b829fe1ef96bd128ad60
RESEARCH PRODUCT
Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1).
Hermann HartmannAndre BongersHeinz Deckersubject
Conformational changeProtein Conformationmedicine.medical_treatmentBiophysicsNeutron scatteringMegathura crenulataBiophysical PhenomenamedicineAnimalsScattering RadiationProtein Structure QuaternaryNeutronsbiologyChemistryScatteringHemocyaninGeneral Medicinebiology.organism_classificationSmall-angle neutron scatteringRespiratory proteinOxygenCrystallographyMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninProtein Bindingdescription
The respiratory protein of the keyhole limpet, Megathura crenulata, the hemocyanin (KLH), commonly used as an immunogen, binds oxygen cooperatively, which implies the existence of different conformations. For the first time, two different conformations of KLH1 were detected upon oxygenation, a deoxy and an oxy state, using small-angle neutron scattering. Rearrangements in the quaternary structure of KLH1 were predicted from the different radii of gyration and the shifts of the minima and maxima in the scattering curves. Upon oxygenation, KLH1 becomes smaller and more compact. Model reconstruction of KLH1 indicates a hollow cylinder with two rings located close to both ends, which move slightly together upon oxygenation.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-10-01 | European biophysics journal : EBJ |