Epinephrine has the following structure. Which of the following amino acids are used by the epinephrine receptor to interact with epinephrine via hydrogen bonds and electrostatic interactions? НО. HO Phe and Gln Ser and Asp O Lys and Tyr O Val and Thr OGlu and Leu OH H H
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- compare the structures of the peptide neurotransmitters Met-enkephalin and Leu-enkephalinShow where trypsin and chymotrypsin would cleave the following peptide. Tyr-Ile-Gln-Arg-Leu-Gly-Phe-Lys-Asn-Trp-Phe-Gly-Ala-Lys-Gly-Gln-GlnB. After treatment with peroxyformic acid, the peptide hormone vasopressin is partially hydrolyzed. The following fragments are recovered. Propose a primary structure for vasopressin.Phe-Gln-Asn Pro-Arg-Gly • NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gln-AsnC. Consider the following peptide: Gly-Ile-Glu-Trp-Thr-Pro-Tyr-Gln-Phe-Arg-LysWhat amino acids and peptides are produced when the above peptide is treated with each of the following reagents?1. Carboxypeptidase2. Chymotrypsin3. Trypsin 4. DNFBD. From the analytical results, deduce the primary structure of a peptide isolated from the Atlantian orchid that contains 14 amino acids.Complete hydrolysis produces the following amino acids: Gly (3), Leu (3), Glu (2), Pro, Met, Lys (2), Thr, Phe. Treatment with carboxypeptidase releases glycine. Treatment with DNFB releases DNP- glycine. Treatment with a…Estimate the binding affi nity of a ligand for its receptor from the followingdata:
- Endocrine Ligand acting on intracellular receptor should be: O Hydrophilic O Hydrophobic O Amphipathic O Macromolecule What kinds of molecules may pass throughThe drug Buckeyium binds to the NMDA receptor at the orthosteric binding site (were glutamate would normally bind). Assume that glycine is already bound, and that magnesium is not blocking the NMDAR ion channel. If the channel does not open as a result of Buckeyium binding than Buckeyium would be considered aBuckeyium is a medication that binds to the NMDA receptor at the orthosteric binding site (were glutamate would normally bind). Assume glycine is already bonded and magnesium isn't inhibiting the NMDAR ion channel. Buckeyium would be regarded a poison if the channel did not open as a consequence of its binding.
- The NMDA receptor I/V curve is nonlinear, why? What about the GluA2-containing AMPA receptor I/V curve? Draw both under normal physiological conditions. In addition, explain what happens for the NMDA receptor I/V curve when you lower the magnesium concentration.The Table below shows the names of proteins whose functions are regulated through the binding of their ligands. Complete this Table by filling in the correct ligands for each of the proteins, the corresponding K, value, the affinity of this protein for its ligand and the source where the protein is found. Example Protein Avidin 1 Insulin receptor 2 Anti-HIV immunoglobulin 3 Nickel binding protein 4 Myoglobin 5 Myosin 6 Acetyl-CoA carboxylase 7 Cannabinoid receptor 1 (CB1) 8 Guanylyl cyclase Ligand Biotin Kd (M) 1 x 10-15 Affinity high Source/Organism Egg whiteEthanol is unusual in that it is freely soluble in both water and lipids. Thus, it has access to all regions of the highly vascularized brain. Although the molecular basis of ethanol action in the brain is not clear, ethanol evidently influences a number of neurotransmitter receptors and ion channels. Suggest a biochemical explanation for the diverse effects of ethanol.
- Chymotrypsin preferentially binds the transition state. What is meant by that?Ligand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.Answer the following step by step A) How many milliliters of 1:100 epinephrine are needed for a 5 mg dose? B) How many milligrams are there in a 1cc dose of 2% Xylocaine? C)You have 20% acetylcysteine; how many milliliters do you need of this to form 4 ml of 8% solution?