When analyzing a PTH (phenylthiohydratoin) derivative of the amino acid isoleucine, resulting from one round of an Edman Degradation experiment, which of the following experimental reverse phase chromatography results would you expect to see? a.)The isoleucine-PTH derivative will elute from the hydrophobic column with a greater retention time relative to most other amino acid-PTH derivatives because it is relatively non polar. b.)The isoleucine-ÞTH derivative will elute from the hydrophobic column with a lesser retention time relative to most other amino acid-PTH adducts because it is relatively polar. c.)The isoleucine-PTH derivative will elute from the hydrophobic column with a retention time in between the groups of polar and non polar amino acid-PTH derivatives because it is neither polar nor non polar.

When analyzing a PTH (phenylthiohydratoin) derivative of the amino acid isoleucine, resulting from one round of an Edman Degradation experiment, which of the following experimental reverse phase chromatography results would you expect to see? a.)The isoleucine-PTH derivative will elute from the hydrophobic column with a greater retention time relative to most other amino acid-PTH derivatives because it is relatively non polar. b.)The isoleucine-ÞTH derivative will elute from the hydrophobic column with a lesser retention time relative to most other amino acid-PTH adducts because it is relatively polar. c.)The isoleucine-PTH derivative will elute from the hydrophobic column with a retention time in between the groups of polar and non polar amino acid-PTH derivatives because it is neither polar nor non polar.

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter28: High-performance Liquid Chromatography

Section: Chapter Questions

Problem 28.19QAP

See similar textbooks

Similar questions

Explain how we would run a paper chromatography on an amino acid sample (explain the procedure or method). In a paper chromatography of an amino acid, the solvent front traveled 12.0 cm while the amino acid traveled 6.0 cm. What is Rf value of the amino acid?
Doe hydrophobic silica gel act as non-polar stationary phase in TLC making the process as reverse chromatography? explain
Chemistry how would you isolate the glycosylated insulin from the unglhcosylated forms? can you come up with a method to purify the protein (insulin with sugar group)? It can be a column or a combination of columns. (hint: use size exclusion chromatography or other method and affinity concept.)
Are the number of spots shown on SDS-PAGE electrophoresis dependant on whether the protein is a monomer or tetramer?
1. A mixture of proteins (pepsinogen, myoglobin, and cytochrome c) is subjected to anion exchange chromatography at pH 5.0. In what order would the following proteins be eluted from the DEAE cellulose anion exchanger by an increasing salt gradient: cytochrome c (pl, 10.6), pepsinogen (pl, 1.0) and myoglobin (pl, 6.8)
A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy). When you ran this protein directly on reversed phase-HPLC with UV monitor set at 280 nm, two peaks were resolved. Mass spec determined that the peaks represented Chain A and Chain B, respectively. The peak area is 500,000 for Peak A (Chain A) and 100,000 for Peak B (Chain B). The molecular masses of Chain A and Chain B are 25,000 and 5000, respectively. The extinction coefficients for Chain A and Chain B are 1 mL/mg.cm and 0.5 mL/mg.cm, respectively. Please calculate x/y.
A protein with a pI of 7.5 will be purified using ion-exchange chromatography. Which ion exchange resin is suitable to use if the buffer has a pH of 7.0?a. A resin with a quaternary amino groupb. A resin with sulfonic acid groupc. A resin containing primary aromatic/aliphatic amino groupd. A resin that has carboxylic acid group
The following are the methods for visualizing spots in TLC chromatogram EXCEPT Choices: Illumination with ultraviolet lamp Using an adsorbent layer that contains a trace of fluorescent dye Treatment of Reagent (e.g. Iodine vapor) None of the above
Consider stereoisomers. What type of isomers would you expect would and what types could not be separted by chromatography techniques. also include specifically thin layer chromotography and why, explain
Seperation of Amino Acids by thin layer chromotography Lab. Please answer #12 and #13 as I am very confused. Thank you for your help!
Protein ABC is a heme-containing protein responsible in electron transfer in microalgae. The target protein was extracted using ammonium sulfate fractional precipitation and quantified using Bradford assay. A set of solutions with increasing concentration was prepared using 15.00 mg/mL analogous protein standard [refer to succeeding table]. Each solution was treated with 80 μL of Bradford reagent and diluted to 1.500mL. The absorbance at 595 nm of each solution was obtained and presented below. Volume of protein std, μL A595 0 0.0002 10 0.0007 25 0.0075 50 0.0165 100 0.0356 250 0.0930 500 0.1950 750 0.3010 1000 0.4175 Report the equation of the calibration curve and proof of linearity (R2 value).
For the three tripeptides TED, RAY and ALI, determine in which order they will be eluted at pH 7.0 from cation exchange chromatography column.