1. Dehydrogenase with H₂N-KKRRRPRPKPAPASAMEWANTWENTY...-COOH a. Provide the amino acid sequence of the signal peptide b. Where will this polypeptide be transported? C. What is the receptor protein of the signal sequence?
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- What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed valuesShow 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…In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacid
- A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0Hydrolysis of β-endorphin (a peptide containing 31 amino acid residues) produces the following amino acids: Tyr 1), Gly 3), Phe 2), Met, Thr 3), Ser 2), Lys 5), Gin 2), Pro, Leu 2), Val 2), Asn 2), Ala 2), lle, His, and Glu Treatment with carboxypeptidase liberates Gln. Treatment with DNFB liberates DNP-Tyr. Treatment with trypsin produces the following peptides: Lys, Gly—Gln, Asn—Ala—He—Val—Lys, Tyr—Gly—Gly—Phe—Met—Thr—Ser—Glu—Lys, Asn—Ala—His—Lys, Ser—Gln—Thr—Pro—Leu— Val—Thr—Leu—Phe—Lys Treatment with chymotrypsin produces the following peptides: Lys—Asn—Ala—He—Val—Lys—Asn—Ala—His—Lys—Lys—Gly—Gln Tyr—Gly—Gly—Phe Met—Thr—Ser—Glu—Lys—Ser—Gin—Thr—Pro—Leu—Val—Thr—Leu—Phe What is the primary sequence of β-endorphin?If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?SIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Protease with mannose-6-phosphate Where is the receptor for this protein located? Where is the final destination of this polypeptide? What happens to the receptor after protein transport?
- Why different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)Need help, please. Draw an oxygen binding curve of Hb at a pH of 7.4 and another curve where all 2,3 BPG has been removed Draw an oxygen binding curve of Hb at a pH of 7.4 and another at pH. Draw an oxygen binding curve of Hb at a pH of 7.4 and another with a mutant Hb in which the predominant form of the protein is monomeric
