1. What is the N-terminal AA residue? 2. What is the C-terminal AA residue? 3. What is the sequence of Peptide 1?
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- A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrezine Nonapeptide Acid Hydrolysis (4 N HCI) at 110 C (2) Arg. Gin, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrolluorobenzene DNP-Thr Gin and Peptide 1 (Arg. Thr, Ser) modified free amino acids Cleavoge with Trypsin, then thrometography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide (yenegen bromide Dipeptide Cleovoge with Chymetrypsin, then chromatography Peptide 3 (Arg, Ser, Tyr, Thr) Amino acid Peptide 4 (Gly, Arg, Tyr) When answering the questions below, please use the one-letter code for the amino acid, with NO spaces and symbols between each letter. 1. What is the N-terminal AA residue? 2. What is the C-terminal AA residue? 3. What is the sequence of Peptide 1? 4. What is the sequence of Peptide 4? 5. What is the overall amino acid…A NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 "C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free Peptide 1 (Arg, Thr, Ser) amino acids Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-A
- (a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO, H N -C- COOH H O,N CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes. octapeptide sequence:A nonapeptide was determined to have the following amino acid composition: (Lys)2, (Gly) 2, (Phe) 2, His, Leu, Met. The native peptide was incubated with 1-fluoro-2,4- dinitrobenzene (FDNB) and then hydrolyzed; 2,4-dinitrophenylhistidine was identified by HPLC. When the native peptide was exposed to cyanogen bromide (CNBr), an octapeptide and free glycine were recovered. Incubation of the native peptide with trypsin gave a pentapeptide, a tripeptide, and free Lys. 2,4-Dinitrophenyl-histidine was recovered from the pentapeptide, and 2,4-dinitrophenylphenylalanine was recovered from the tripeptide. Digestion with the enzyme pepsin produced a dipeptide, a tripeptide, and a tetrapeptide. The tetrapeptide was composed of (Lys) 2, Phe, and Gly. The native sequence was determined to be: Met-Leu-Phe-Lys-Phe-Gly-Gly-Lys-His His-Leu-Gly-Lys-Lys-Phe-Phe-Gly-Met His-Phe-Leu-Gly-Lys-Lys-Phe-Met-Gly Gly-Phe-Lys-Lys-Gly-Leu-Met-Phe-His ● His-Leu-Phe-Gly-Lys-Lys-Phe-Met-Gly
- The following data were obtained from partial cleavage and analysis of an octapeptide: Composition: Ala, Gly2, Lys, Met, Ser, Thr, Tyr CNBr: (1) Ala, Gly, Lys, Thr(2) Gly, Met, Ser, Tyr Trypsin: (1) Ala, Gly(2) Gly, Lys, Met, Ser, Thr, Tyr Chymotrypsin: (1) Gly, Tyr(2) Ala, Gly, Lys, Met, Ser, Thr N terminus: Gly C terminus: Gly Determine the sequence of the peptide.An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO2 H H N C COOH ON- CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes.The tripeptide +H3N-Leu-His-Glu-COO- has pKa values of 2.2, 3.6, 6.0 and 9.1. The isoelectric point (pI) for this peptide will be: 8 5 6 4 None of the above
- Mixtures of amino acids can be analyzed by first separating the mixture into its components through ionexchange chromatography. Amino acids placed on a cation-exchange resin containing sulfonate ( -SO3-) groups flow down the column at different rates because of two factors that influence their movement: (1) ionic attraction between the sulfonate residues on the column and positively charged functional groups on the amino acids, and (2) aggregation of nonpolar amino acid side chains with the hydrophobic backbone of the polystyrene resin. For each pair of amino acids listed, determine which will be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Aspartate and lysine (b) Arginine and methionine(c) Glutamate and valine (d) Glycine and leucine (e) Serine and alanineGiven the following peptides below, what would be more soluble at the indicated pH? 1. (Gly)20 or (Glu)20 in pH 7.0 2. (Lys-Ala)3 or (Phe-Met)3 in pH 7.0 3. (Gly)20 or (Glu)20 in pH 6.0|| 4. (Ala-Ser-Gly)s or (Asn-Ser-His)s in pH 6.0 5. (Ala-Asp-Gly)8 or (Asn-Ser-His)8 in pH 3.0a) Identify and describe the different PEGylation strategies you can use to PEGylate this peptide and draw the chemical structure of the resulting mPEG peptide conjugates. ( draw functional PEGs and corresponding PEGylated products) b) discuss the reaction conditions needed to carry out the PEGylation reactions and explain how pH affects the selectivity of these reactions