The peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this process, the products that are generated are: O PTH-Leu, PTH-Cys, PTH-Arg. PTH-Ser, PTH-Gn, and PTH-Met O PTH-Leu-Cys-Arg-Ser-Gin-Met O PTH-Met and Leu-Cys-Arg-Ser-Gln-Met O PTH-Leu-Cys and PTH-Arg-Ser-Gin-Met O PTH-Leu and Cys-Arg-Ser-Gin-Met
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A: The given peptide sequences are: CNBr 1: Gly-Thr-Lys-Ala-Glu CNBr 2: Ser-Met Tryp 1:…
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Q: A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin…
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- Show the peptides that would result from cleavage by the indicated reagent: a. Val-Arg-Gly-Met-Arg-Ala-Ser by carboxypeptidase A b. Ser-Phe-Lys-Met-Pro-Ser-Ala-Asp by cyanogen bromide c. Arg-Ser-Pro-Lys-Lys-Ser-Glu-Gly by trypsinA sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin, and the other with cyanogen bromide. Given the following sequences of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment: Asn-Thr-Trp-Met-Ile-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen Bromide treatment: Gln-Phe Ile-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-MetConsider the following peptide sequence: Lys-Leu-Ile-Cys-Lys What is the net charge of this sequence at physiological pH? a. -2 b. +1 c. 0 d. -1 e. +2
- Draw the peptide at a pH @1 of Cys-His-Glu-Met-Ile-Ser-Thr-Arg-TyrSickle cell anemia is caused by a point mutation in the β-globin chain of hemoglobin. Glutamic acid is replaced by Valine. HBB sequence in normal adult hemoglobin (Hb A): Leu-Thr-Pro-Glu-Glu-Lys-Ser HBB sequence in mutant adult hemoglobin (Hb S): Leu-Thr-Pro-Val-Glu-Lys-Ser What effect does this mutation have on the structure and function of the protein? Predict what would happen to the RBC if the glutamic acid was replaced with asparagine instead of valine.Multisubunit proteins in which some or all of the subunitsare identical are referred to as _______________________.
- TPA protein function. Use at least two sentences to describe the function of the TPA protein.Draw a peptide for cys-asn- pro-gly (Using the same format in picture)Vasopressin: CYFQNCPRG Oxytocin: CYIQNCPLG Both of these peptides will react with reducing agents such as beta mercaptoethnol (BME). What side group reacts with this reducing agent? What does the fact that these peptides both react with BME tell you about the side groups and therefore this peptide?
- After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride, trypsin will cleave the polypeptide only on the C-side of arginine.) Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?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…Synthesis of peptide bonds is [exorgonic or endergonic]. Thus in isolation, this reaction would [occur or not occur] in cells. Peptide synthesis at the ribosome is coupled to GTP hydrolysis which is an [exergonic or endergonic] process thus making the overall process of synthesizing peptides [spontaneous or not spontaneous].