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DyBOBS: A Dynamic Biomimetic Assay for Odorant-Binding to Odor-Binding Protein

Chemosensory Perception, 2010
An in vitro system was developed to mimic the structural and flow conditions of the human olfactory epithelium and to measure the dynamics of odorant-binding to odor-binding protein (OBP). A hydrophilic fused silica capillary, coated internally with a thin (about 1.3 µm) aqueous film of recombinant rat-OBP3 mimicked the human olfactory epithelium ...
Yabuki, Masayuki   +4 more
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Odorant-Binding Proteins

Critical Reviews in Biochemistry and Molecular Biology, 1994
Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Immunocytochemistry of Odorant-Binding Proteins

1994
Odorant-binding proteins are small water-soluble proteins that have been detected in the perireceptor compartment of olfactory receptor cells of vertebrates and insects [1,2]. Although their definite physiological role in olfaction is still unclear, similar functions have been proposed in stimulus transport or inactivation [1–6].
Steinbrecht, R.   +3 more
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Electrochemical biosensing with odorant binding proteins

2020
The development of sensors that mimic the natural smell sensing mechanism and selectively recognizes the odorants remains highly challenging. Electrochemical based sensing approaches aiming at monitoring molecular recognition events between surface receptors and analytes in solution or in the gas phase, are one possible transduction platforms among ...
Szunerits, Sabine   +2 more
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Deswapping bovine odorant binding protein

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008
The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121.
RAMONI, Roberto   +6 more
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Odorant binding proteins of Heliothis virescens

Insect Biochemistry and Molecular Biology, 1993
cDNA clones coding for three different binding proteins were isolated from an antennal library of Heliothis virescens. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a comparison with the predicted primary structures of antennal binding proteins from different moth ...
J, Krieger   +3 more
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Odorant Binding to Bovine Odorant Binding Protein Detected by Intrinsic Fluorescence

Chemistry Letters, 2005
Abstract Odorant binding to bovine odorant binding protein (OBPb) made OBPb structure a little tighter and odorant detection by intrinsic fluorescence possible. For odorant with high affinity such as 3,7-dimethyl-1-octanol (DMO), the binding reaction proceeded in a two-step manner that inferred an existence of a third binding site.
Mineo Ikematsu   +2 more
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Stability and Dynamics of the Porcine Odorant-Binding Protein

Biochemistry, 2007
The denaturation process of porcine odorant-binding protein (pOBP) was studied by intrinsic fluorescence analysis and far- and near-UV circular dichroism measurements. Our results showed that a reversible one-step process described the denaturation by GdnHCl.
Staiano M   +8 more
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Odorant‐Binding Proteins: Structural Aspects

Annals of the New York Academy of Sciences, 1998
ABSTRACT: Structural data on odorant‐binding proteins (OBPs), both in vertebrates and in insects, are reviewed and discussed. OBPs are soluble proteins interacting with odor molecules and Pheromones in the perireceptor areas, the nasal mucus in vertebrates and the sensillar lymph in insects.
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Odorant‐Binding Proteins: Expression and Function

Annals of the New York Academy of Sciences, 1998
ABSTRACT: Odorant‐binding proteins (OBPs) are a major constituent of the aqueous perireceptor compartment in vertebrates and in insects. Although different in primary structure, they are supposed to serve similar functions in both animal groups: (i) OBPs may act as solubilizers and carriers of the lipophilic odorants in the aqueous mucus or sensillum ...
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