2.) An unknown amino acid was subjected to paper chromatography with five amino acid standards in order to identify it. After visualization using ninhydrin, the distances travelled were measured as follows: Distances: Solvent 9.3cm A - 1.1cm B - 4.7cm C - 2.4cm D - 7.6cm E - 8.7cm X - 1.6cm Arrange the amino acids from most non-polar to least non-polar. Sample Rf Value Polarity A B E What is the possible identity of the unknown amino acid? Answer can be up to two amino acids.

2.) An unknown amino acid was subjected to paper chromatography with five amino acid standards in order to identify it. After visualization using ninhydrin, the distances travelled were measured as follows: Distances: Solvent 9.3cm A - 1.1cm B - 4.7cm C - 2.4cm D - 7.6cm E - 8.7cm X - 1.6cm Arrange the amino acids from most non-polar to least non-polar. Sample Rf Value Polarity A B E What is the possible identity of the unknown amino acid? Answer can be up to two amino acids.

Organic Chemistry

8th Edition

ISBN:9781305580350

Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Publisher:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. Foote

Chapter27: Amino Acids And Proteins

Section27.4: Primary Structure Of Polypeptides And Proteins

Problem 27.6P: Deduce the amino acid sequence of an undecapeptide (11 amino acids) from the experimental results...

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Similar questions

Considering the peptide structure on the image, label N-terminus and C-terminus, circle each of the peptide (amide) bonds, and provide the primary sequence of the protein using three letter abreviaciones for the amino acids
Why is glycine the only amino acid commonly observed in peptides inconformations with phi and psi values which are not restricted to the values in the Ramachandran plot below?
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
Which separation technique is the most specific and offers the highest protein purification possible?
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.
Consider the peptide EAHIVR. Write out the sequence of the peptide from N to C in three letter code. Draw the complete structure of the peptide including all peptide bonds and side chains at pH 8.0. Calculate the pI of this peptide. Calculate the net charge of this peptide at pH 2, pH 7, and pH 11. *please show math for # 3 and #4 pls*
The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured. Classify the following processes according to the denaturing agent involved. Please help me understand the diff and correct any mistakes.
In a paragraph form provide the experimental procedure of the reaction of oxazetidine-containing peptides and α-ketoacid that will result in protein that contain native serine residues
Use the following chromatogram of standard amino acids: Which of the following statements BEST describe the given chromatogram? Peaks 14, 18, 20 and 22 have the lowest concentrations and highest affinity to the mobile phase. The peaks are narrow and show clear separation of the mixture. Peaks 4, 5, 11 and 24 have the highest concentrations in the mixture and highest affinity to the mobile phase. The peaks are narrow and show suboptimal conditions for separation.
Given the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in Table (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.
a) A solution of amino acid having carboxylic side chain was titrated against NaOH. If initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5.b) Briefly explain how you will separate amino acids mixture using the charge difference between the amino acids. c) A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that pKa1 and pKa2 of glycine are 2.34 and 9.60, respectively. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid, if [x] and [y] are the concentrations of dissociated and undissociated amino acid, respectively.
Finally, you want to make completely certain that you purified the correct protein and not some other protein (like biochemisnotfunase). To confirm the identity of your protein, you run a Western blot. When doing a Western, one typically needs a solution of phosphate-buffered saline, which is comprised of 10 mM phosphate buffer(pH 8.0) and 0.9% (w/v) NaCl. Describe how you would make 500 mL of this solution including the grams of sodium phosphate, monobasic and sodium phosphate, dibasic that you would need. Making the phosphate buffer is a little tricky. Be sure to use the correct ratio of monobasic and dibasic sodium phosphate to get the correct pH. The Henderson- Hasselbalch equation might come in handy here. Finally, the molecular weight of sodium phosphate, monobasic (NaH2PO4) is 119.98 g/mol and the molecular weight of sodium phosphate, dibasic (Na2HPO4) is 141.96 g/mol.