Which method of chromatography would be the most appropriate for separating mixtures of the following peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA (b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE (c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5? Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–Val Peptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-Ile Peptide 2: Arg–Ile–Pro–Lys–Cys–Met–Lys

Which method of chromatography would be the most appropriate for separating mixtures of the following peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA (b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE (c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5? Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–Val Peptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-Ile Peptide 2: Arg–Ile–Pro–Lys–Cys–Met–Lys

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter1: Relative Value, Addition, And Subtraction Of Decimals

Section: Chapter Questions

Problem 39SST

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(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.
(b) Why does solution pH affect separation of proteins via electrophoresis? (c) With reference to a labelled diagram, what is the principle of separation via capillary zone electrophoresis (CZE)?
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
A peptide was analyzed with the following results. Whatis the primary sequence of the peptide? Briefly state the conclusions of each experimental result and indicate your logic. a)Mass spectrometry was consistent with a peptide of 7 amino acids containing W,C,D,M,N,K, and I. b)One cycle of Edman degradation of the peptide yielded a single product, the PTH derivative of I c)Cleavage of the peptide with CNBr yielded two products. One contained 5 amino acids, and the other 2. One cycle of Edman degradation yielded the PTH derivatives of Iand N, respectively. d)Treatment of the peptide with trypsin yielded 2 products. One of them had significant light absorbance at 280 nm, and Edman degradation yielded the PTH derivative of I. The other trypsin-generated product contained 4 amino acids, and Edman degradation yielded the PTH derivative of Asp.
What is the basis for the separation of proteins by the following techniques? (a) gel-filtration chromatography(b) affinity chromatography(c) ion-exchange chromatography
What is the basis for the separation of proteins by the following techniques? (a) gel-filtration chromatography (b) affinity chromatography (c) ion-exchange chromatography (d) reverse phase HPLC
An ion-exchange chromatographic separation is performed using a diethyl-aminoethyl- (DEAE)-sepharose column to separate proteins in a mixture. The mixture contains Protein A (pl=6.0), B (pl35.0), C (pl=7.5), D (pl =1), and E (pl=4.0). The protein mixture is prepared in a buffer solution pH =5. When the protein mixture is loaded onto the column, and the column is washed with a buffer solution pH 5, which protein(s) will be captured by DEAE-sepharose in the column? O Protein B because it is predominantly in net negative charge form. O Proteins D and E because they have predominately net negative charge in pH 5 solution O Proteins A, C, D and E because they have charges O Proteins A and C because both both predominantly have net positive charges O Proteins Band E because both predominantly have net positive charges
An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?
What is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).
The sequence of a peptide is given below. YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE If you perform peptide sequencing by tandem mass spectroscopy, calculate the predicted m/z ratio for b1, b5, b12, y1, y5 and y12 ions.
1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
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