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Awan, Ali: In Silico Transfer of Ligand Binding Function between Structurally Analogous Proteins
Awan, Ali: In Silico Transfer of Ligand Binding Function between Structurally Analogous Proteins

... function between structurally analogous proteins is only as feasible as the computational methods are accurate. That is to say, the hybrids resulting from the in silico engineering will only resemble their empirically determined counterparts as far as the protein folding, energy minimisation and pro ...
Whey Protein Concentrate
Whey Protein Concentrate

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The Real Story Behind the Amino Acid Leucine
The Real Story Behind the Amino Acid Leucine

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Nuclear receptor ligand-binding domains: three

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One of the most famous examples
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Teagasc PhD Walsh Fellowship
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Chapter 5 Polypeptides Geometry of Peptide Bond
Chapter 5 Polypeptides Geometry of Peptide Bond

... protein to unfold to an extended structure. The SDS molecules bind to the extended structure at a ratio of about 1 SDS molecule for each amino acid residue, or about 1.4 g SDS per g protein. Rod- like structures are formed, where the charge along the rod is uniformly negative from the sulfate anions ...
Lab.-7-Western Blotting
Lab.-7-Western Blotting

... biological fluids and proteins secreted in vitro, are open to analysis by Western blotting • In most cases, the cells are harvested, washed, and lysed to release the target protein • For best results, all these steps should be carried out on ice • This will minimize proteolysis, dephosphorylation, a ...
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G protein–coupled receptor



G protein–coupled receptors (GPCRs), also known as seven-transmembrane domain receptors, 7TM receptors, heptahelical receptors, serpentine receptor, and G protein–linked receptors (GPLR), constitute a large protein family of receptors that sense molecules outside the cell and activate inside signal transduction pathways and, ultimately, cellular responses. Coupling with G proteins, they are called seven-transmembrane receptors because they pass through the cell membrane seven times.G protein–coupled receptors are found only in eukaryotes, including yeast, choanoflagellates, and animals. The ligands that bind and activate these receptors include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters, and vary in size from small molecules to peptides to large proteins. G protein–coupled receptors are involved in many diseases, and are also the target of approximately 40% of all modern medicinal drugs. Two of the United States's top five selling drugs (Hydrocodone and Lisinopril) act by targeting a G protein–coupled receptor. The 2012 Nobel Prize in Chemistry was awarded to Brian Kobilka and Robert Lefkowitz for their work that was ""crucial for understanding how G protein–coupled receptors function."". There have been at least seven other Nobel Prizes awarded for some aspect of G protein–mediated signaling.There are two principal signal transduction pathways involving the G protein–coupled receptors: the cAMP signal pathway and the phosphatidylinositol signal pathway. When a ligand binds to the GPCR it causes a conformational change in the GPCR, which allows it to act as a guanine nucleotide exchange factor (GEF). The GPCR can then activate an associated G protein by exchanging its bound GDP for a GTP. The G protein's α subunit, together with the bound GTP, can then dissociate from the β and γ subunits to further affect intracellular signaling proteins or target functional proteins directly depending on the α subunit type (Gαs, Gαi/o, Gαq/11, Gα12/13).
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