Abstract
In the present work, we study the effect of odorant binding on the thermal stability of odorant binding protein 14 (OBP14) of the honey bee (Apis mellifera L.). Thermal denaturation of the protein in the absence and presence of different odorant molecules was monitored by Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD). FT-IR spectra show characteristic bands for intermolecular aggregation through formation of intermolecular b-sheets during the heating process. Transition temperatures in the FT-IR spectra were evaluated using moving-window 2D
correlation maps and confirmed by CD measurements. The obtained results reveal an increase of the denaturation temperature of the protein when bound to an odorant molecule. We could also discriminate between high and low affinity odorants using transition temperatures, as demonstrated independently by the two applied methodologies. The increased thermal stability in the presence of ligands is attributed to a stabilizing effect of non-covalent interactions between OBP14 and the odorant molecule
Originalsprache | Englisch |
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Publikationsstatus | Veröffentlicht - 2013 |
Veranstaltung | Soft Control - Dauer: 22 Sept. 2013 → 24 Sept. 2013 |
Konferenz
Konferenz | Soft Control |
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Zeitraum | 22/09/13 → 24/09/13 |
Research Field
- Biosensor Technologies