What is the secondary structure of the peptide hormone GLP-1
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a) What is the secondary structure of the peptide hormone GLP-1?
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- What is the biological function of the Neurofibromin-1 (NF1) protein?What is glucagon-like peptide-1 (GLP-1) ?Show 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…
- A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr. Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase. What is the amino acid sequence of this polypeptide?A mutant form of polypeptide hormone has the following amino acid composition: Asp, Arg, lle, Met, Phe, Pro, Tyr, Val The following observations are made: Trypsin yields a dipeptide containing Asp and Arg, and a hexapeptide with all the rest. Cyanogen bromide cleavage yields a dipeptide containing Phe and Pro, and a hexapeptide containing all the others. Chymotrypsin cleaves the hormone into two tetrapeptides with the following composition: (Asp, Arg, Tyr, Val) and (lle, Met Phe, Pro) What is the amino acid sequence of this polypeptide?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. 3) Which of the proteins demonstrate the tightest/strongest binding of the hormone? Which demonstrates the least tight binding of the hormone? What is the basis for your answer?
- Two melanocyte-stimulating hormones have the following amino acid sequences. Take a highlighter or colored pencil, and figure out how much of the sequence the porcine MSH has in common with the human MSH (how much is conserved between the two species). beta-MSH (human): Ala-Glu-Lys-Lys-Asp-Glu-Gly-Pro-Tyr-Arg-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp beta-MSH (porcine): Asp-Glu-Gly-Pro-Tyr-Lys-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp One amino acid interrupts the parts you highlighted in each sequence. Which amino acid was it in each and which category does that amino acid belong to on your amino acid chart? this to make much difference for the cross-species function of beta-MSH (why?)? and Do you expectWhat is glucocorticoid receptor ?the key features between glycosaminoglycan-binding proteins and lectins?
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