scholarly journals A large-scale expression strategy for multimeric extracellular protein complexes using Drosophila S2 cells and its application to the recombinant expression of heterodimeric ligand-binding domains of taste receptor

2017 ◽  
Vol 26 (11) ◽  
pp. 2291-2301 ◽  
Author(s):  
Atsuko Yamashita ◽  
Eriko Nango ◽  
Yuji Ashikawa
Keyword(s):  
Ligand Binding ◽  
Large Scale ◽  
Protein Complexes ◽  
Recombinant Expression ◽  
Taste Receptor ◽  
Extracellular Protein ◽  
S2 Cells ◽  
Binding Domains ◽  
Drosophila S2 Cells

scholarly journals Differential scanning fluorimetric analysis of the amino-acid binding to taste receptor using a model receptor protein, the ligand-binding domain of fish T1r2a/T1r3

2019 ◽  
Author(s):  
Takashi Yoshida ◽  
Norihisa Yasui ◽  
Yuko Kusakabe ◽  
Chiaki Ito ◽  
Miki Akamatsu ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ligand Binding ◽  
Taste Receptor ◽  
Thermal Stabilization ◽  
Receptor Protein ◽  
Binding Characteristics ◽  
Melting Temperatures ◽  
Binding Domains ◽  
Amino Acid Binding

AbstractTaste receptor type 1 (T1r) is responsible for the perception of essential nutrients, such as sugars and amino acids, and evoking sweet and umami (savory) taste sensations. T1r receptors recognize many of the taste substances at their extracellular ligand-binding domains (LBDs). In order to detect a wide array of taste substances in the environment, T1r receptors often possess broad ligand specificities. However, the entire ranges of chemical spaces and their binding characteristics to any T1rLBDs have not been extensively analyzed. In this study, we exploited the differential scanning fluorimetry (DSF) to medaka T1r2a/T1r3LBD, a current sole T1rLBD heterodimer amenable for recombinant preparation, and analyzed their thermal stabilization by adding various amino acids. The assay showed that the agonist amino acids induced thermal stabilization and shifted the melting temperatures (Tm) of the protein. An agreement between the DSF results and the previous biophysical assay was observed, suggesting that DSF can detect ligand binding at the orthosteric-binding site in T1r2a/T1r3LBD. The assay further demonstrated that most of the tested L-amino acids, but no D-amino acid, induced Tm shifts of T1r2a/T1r3LBD, indicating the broad L-amino acid specificities of the proteins probably with several different manners of recognition. The Tm shifts by each amino acid also showed a fair correlation with the responses exhibited by the full-length receptor, verifying the broad amino-acid binding profiles at the orthosteric site in LBD observed by DSF.

scholarly journals Process Simulation and Techno-Economic Analysis of Large-Scale Bioproduction of Sweet Protein Thaumatin II

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 838
Author(s):  
Kirolos D. Kelada ◽  
Daniel Tusé ◽  
Yuri Gleba ◽  
Karen A. McDonald ◽  
Somen Nandi
Keyword(s):  
Economic Analysis ◽  
Process Simulation ◽  
Large Scale ◽  
Recombinant Expression ◽  
Molecular Farming ◽  
Consumer Preference ◽  
Production Method ◽  
Long Term Effects ◽  
Adverse Health Effects ◽  
Sweet Proteins

There are currently worldwide efforts to reduce sugar intake due to the various adverse health effects linked with the overconsumption of sugars. Artificial sweeteners have been used as an alternative to nutritive sugars in numerous applications; however, their long-term effects on human health remain controversial. This led to a shift in consumer preference towards non-caloric sweeteners from natural sources. Thaumatins are a class of intensely sweet proteins found in arils of the fruits of the West-African plant Thaumatococcus daniellii. Thaumatins’ current production method through aqueous extraction from this plant and uncertainty of the harvest from tropical rainforests limits its supply while the demand is increasing. Despite successful recombinant expression of the protein in several organisms, no large-scale bioproduction facilities exist. We present preliminary process design, process simulation, and economic analysis for a large-scale (50 metric tons/year) production of a thaumatin II variant using several different molecular farming platforms.

scholarly journals Upstream – News in Genomics

2002 ◽  
Vol 3 (3) ◽  
pp. 221-225
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ovarian Cancer ◽  
Oryza Sativa ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Proteomic Analysis ◽  
Large Scale ◽  
Protein Complexes ◽  
The Other ◽  
Blood Samples

In recent months a bumper crop of genomes has been completed, including the fission yeast (Schizosaccharomyces pombe) and rice (Oryza sativa). Two large-scale studies ofSaccharomyces cerevisiaeprotein complexes provided a picture of the eukaryotic proteome as a network of complexes. Amongst the other stories of interest was a demonstration that proteomic analysis of blood samples can be used to detect ovarian cancer, perhaps even as early as stage I.

scholarly journals Paired opposing leukocyte receptors recognizing rapidly evolving ligands are subject to homogenization of their ligand binding domains

2011 ◽  
Vol 63 (12) ◽  
pp. 809-820 ◽  
Author(s):  
Sigbjørn Fossum ◽  
Per Christian Saether ◽  
John Torgils Vaage ◽  
Michael Rory Daws ◽  
Erik Dissen
Keyword(s):  
Ligand Binding ◽  
Binding Domains ◽  
Leukocyte Receptors

scholarly journals Biochemical and NMR Mapping of the Interface between CREB-binding Protein and Ligand Binding Domains of Nuclear Receptor

2004 ◽  
Vol 280 (7) ◽  
pp. 5682-5692 ◽  
Author(s):  
Fabrice A. C. Klein ◽  
R. Andrew Atkinson ◽  
Noelle Potier ◽  
Dino Moras ◽  
Jean Cavarelli
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptor ◽  
Binding Protein ◽  
Creb Binding Protein ◽  
Binding Domains

Validating the predictions of murburn model for oxygenic photosynthesis: Analyses of ligand-binding to protein complexes and cross-system comparisons

2021 ◽  
pp. 1-33
Author(s):  
Kelath Murali Manoj ◽  
Daniel Andrew Gideon ◽  
Abhinav Parashar ◽  
Vijay Nirusimhan ◽  
Pushparaj Annadurai ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Protein Complexes ◽  
Oxygenic Photosynthesis ◽  
Cross System
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