ArticleEuropean biophysics journal : EBJ2014
Honey bee odorant-binding protein 14: effects on thermal stability upon odorant binding revealed by FT-IR spectroscopy and CD measurements.
Article in European biophysics journal : EBJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 27 citations in OpenAlex.
- Responses of the Pheromone-Binding Protein of the Silk MothSensors (Basel, Switzerland) · 2021Article
- Biosensors to Monitor Water Quality Utilizing Insect Odorant-Binding Proteins as Detector Elements.Biosensors · 2019Article
- Odorant-Binding Proteins as Sensing Elements for Odour Monitoring.Sensors (Basel, Switzerland) · 2018Review
- Structural Transformation Detection Contributes to Screening of Behaviorally Active Compounds: Dynamic Binding Process Analysis of DhelOBP21 from Dastarcus helophoroides.Journal of chemical ecology · 2017Article
- Multiple Binding Poses in the Hydrophobic Cavity of Bee Odorant Binding Protein AmelOBP14.Journal of chemical information and modeling · 2015Article
- Electronic Olfactory Sensor Based on A. mellifera Odorant-Binding Protein 14 on a Reduced Graphene Oxide Field-Effect Transistor.Angewandte Chemie (International ed. in English) · 2015Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
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Abstract
In the present work, we study the effect of odorant binding on the thermal stability of honey bee (Apis mellifera L.) odorant-binding protein 14. 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 the formation of intermolecular β-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 by determining 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 odorant-binding protein 14 and the odorant molecule.
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