1) What is the charge state of the peptide in pH7 water solution? a GKEAPLCKR
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- The following amino acids that are often found inside globulin molecules are () A, Tyr B, Phe C, Asn D, Glu True of false 1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first synthesized and then corresponding nucleotides are formed with phosphoribose. () 2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5 'end to the 3' end. () 3. The change of protein conformation is caused by the breaking of covalent bonds within the molecule. () 4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. () 5. The active center of an enzyme usually consists of several amino acid residues adjacent to each other in the primary structure. (). The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?Snake venom contains many hydrolase enzymes, including several serine proteases. One such protease (present in high concentrations in snake venom) mimics the action of thrombin to activate fibrin. The venom protease cleaves peptide bonds with a specificity for basic, positively charged amino acids. This enzyme is incubated with a substrate peptide with the sequence SNPDCKVALYMTW. Draw a mechanism for the peptide hydrolysis of this specific peptide catalyzed by this snake venom protease. Include the structure of the active site amino acids of the enzyme and the substrate peptide group (including the full structure of the 2 specific amino acids that contribute to the scissile peptide group in the substrate) in your mechanism. Use the curved arrow convention to illustrate the flow of electrons.
- Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by N-acetylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7 The lateral chain of one of these amino acids can be modified by phosphorylation. Write the semi‐developed form of the lateral chain of this modified amino acid at pH 7.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 0A mutant form of polypeptide hormone angiotensin II has the amino acid composition (Asp, Arg, Ile, 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, of composition (Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro) • The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase. What is the sequence of angiotensin II?
- 1. Amino acid analysis of the peptide gave the following residues: Asp Leu Lys Met Phe Tyr. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was C-C-CH2. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a dipeptide, a tetrapeptide and a free Lys. What is the amino acid sequence for this heptapeptide?A mutant form of polypeptide hormone angiotensin II has the amino acidcomposition (Asp, Arg, Ile, Met, Phe, Pro, Tyr, Val)The following observations are made:• Trypsin yields a dipeptide containing Asp and Arg and a hexapeptide withall the rest.• Cyanogen bromide cleavage yields a dipeptide containing Phe and Proand a hexapeptide containing all the others.• Chymotrypsin cleaves the hormone into two tetrapeptides, of composition (Asp, Arg, Tyr, Val) and (Ile, Met, Phe, Pro)• The dipeptide of composition (Pro, Phe) cannot be cleaved by either chymotrypsin or carboxypeptidase.What is the sequence of angiotensin II?Which one of the following would best allow us to conclude that the rate of chymotrypsin was pseudo-first-order with respect to the peptide Leu-Phe- Gly, based on our coverage? O None of the other options are suitable because this enzyme catalyzes a reaction with only one substrate. O If the reaction is of the ordered sequential type, with the peptide binding second. O If the concentration of peptide is quite low. O If the peptide concentration is much higher than the Km. O If the reaction is of the ordered sequential type, with the peptide binding first.
- Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides 1. Ile—Val—Cys—Arg—Thr—Gly—Cys—Lys—Asn—Phe—Leu2. Trp—Lys—Cys—Phe—Arg—His—Thr—Lys—Cys—SerTreatment of the intact polypeptide with trypsin yields fragments with the following aminoacid compositions(Arg, Cys2, Ile, Ser, Val)(Arg, Cys2, Gly, Lys, Thr, Phe)(Asn, Leu, Phe)(His, Lys, Thr)(Lys, Trp)Edmands chemistry reveal the following PTH derivatives in equal quantity after cycle 1• PTH--Ile and PTH--Trp a) Rewrite the intact polypeptide, by indicating the positions of the disulfide bonds(Indicate your reasoning) b) How many products do you expect after chymotrypsin cleavage of the intactpolypeptide? c) You are performing an isoelectric focusing experiment (IEF) on a gel with a pH range of 2to 14. Indicate on the diagram below at what point along the gel will peptide 1 abovefocus, in the presence (X) and absence (Y) of DTT. (also show your calculations)You have an unknown heptapeptide that gives the following amino acids after acid hydrolysis (2M.2K,R, A,P) treatment with CNBr gives hormoserine lactone (M*), a tetrapeptide (2K,M*,A) and (P,R). Treatment with trypsin gives free P, free K, (A,K,M) and (R,M). what is the sequence of amino acids for the heptapeptide? show work.Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.