The sample preparation using the EZ:Faast kit involves many steps. Put the following steps in the correct order, first to last. 5 7 4 6 3 2 1 < > > > Extract the derivatised amino acids using a liquid-liquid extraction. The amino acids are in the organic layer. Remove the organic solvent by drying the sample extracts under Nitrogen gas. Derivatise the amino acids using the 'proprietary' derivatising agent. Reconstitute the derivatised amino acids with HPLC mobile phase, prior to assaying them using LC-MS. Elute the amino acids from the SPE media. Use SPE (solid phase extraction) to isolate free amino acids from sample matrix components. Add internal standard.

The sample preparation using the EZ:Faast kit involves many steps. Put the following steps in the correct order, first to last. 5 7 4 6 3 2 1 < > > > Extract the derivatised amino acids using a liquid-liquid extraction. The amino acids are in the organic layer. Remove the organic solvent by drying the sample extracts under Nitrogen gas. Derivatise the amino acids using the 'proprietary' derivatising agent. Reconstitute the derivatised amino acids with HPLC mobile phase, prior to assaying them using LC-MS. Elute the amino acids from the SPE media. Use SPE (solid phase extraction) to isolate free amino acids from sample matrix components. Add internal standard.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Using the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.
An amino acid mixture of phenylalanine, glycine and glutamic acid is to be separated bypaper chromatography. The solvent is less polar than water. Which of these amino acids will have the highest Rf value and which the lowest? Explain. Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino acids, alanine and methionine. What can you deduce about the structure of the protein from these results? Name the amino acids that contribute atoms to both purine and pyrimidine rings.
Draw the structure of the tetrapeptide Asp-Arg-Val-Tyr. Please show the appropriate stereochemistry of the natural amino acids in the resulting peptide. Please draw all ionizable groups in their neutral form.
Electrophoresis of a mixture of lysine, histidine, and cysteine is carried out at pH 7.64. Describe the behavior of each amino acid under these conditions.
. True/ False A. Amino acids found in the living systems are generally in the D-form B. The R-group attached to alfa carbon atom of amino acids are unique for each amino acids. C. Of the 20 essential amino acids, glycine is the only amino acid which is achiral. D. Ions of heavy metals Hg2+ or Pb2+ denature proteins by combining with the amino groups. E. Denaturation of protein involves the breakdown of secondary, tertiary and quaternary structure. F. Cysteine is the only amino acid that can form a disulfide bridge. G. Both the poly saccharides and proteins are polymers. H. Hydrogen bonding is responsible for the secondary structure of Proteins. I. When proteins are hydrolyzed, smaller peptides and amino acids are produced. J. When simple lipids are hydrolyzed glycerol an alcohol as well as fatty acids and their salts are produced.
One of the most advanced methods for determining a protein sequence is tandem mass spectrometry (MS/MS). Select from the list of statements below all that applies to MS/MS. Group of answer choices CID is one way of performing tandem MS experiments The experiment start by chopping the protein into smaller peptide fragments using an enzyme These peptide fragments are later introduced into the mass spectrometer to determine their molecular weight Peptide fragments are selected for further fragmentation by collision with an inert gas There are only 4 types of ions which can result from MS/MS fragmentation: a, b, x, and y ions The a and b ions are the ones with the original C terminus, whereas the x and y ions are the ones with the original N-terminus All of the above
A researcher wishes to obtain a glycoside (an organic compound) from an aqueous plant extract using the solvent extraction technique. She therefore performs the following steps: Step 1: An aqueous solution (100 mL) containing 7 g of the glycoside was shaken with 50 mL of ethyl acetate. Step 2: The resulting aqueous layer from Step 1 was further shaken with 50 mL of dichloromethane. Given that: KD for the glycoside in ethyl acetate-water = 0.8 KD for the glycoside in dichloromethane-water = 0.9 (i)Calculate the total mass of glycoside extracted. (ii)If the molar mass of the glycoside = 784.3 g/mol, calculate the molar concentration of the glycoside remaining in the aqueous layer after each extraction.
How can we determine the following amino acid sequence using different structure analysis methods?
What is the amino terminal residue in this peptide? What is the carboxyl terminal residue in this peptide? The net charge of this peptide at pH 7.4 would be?
Write out a stepwise sequence that shows how a racemic mixture of leucine enantiomers can be resolved into optically active amino acids using (R)-a-methylbenzylamine.
what is The method that would be BEST to use to monitor protein secondary structure during the titration of a denaturing agent?
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