(a)
Interpretation:
The digestion of octapeptide AVGWRVKS with trypsin. The most suitable method for separation of the products between ion-exchange or gel-filtration chromatography should be determined.
Concept introduction:
A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.
(b)
Interpretation:
If the protein was digested with chymotrypsin. The optimal separation method should be explained.
Concept introduction:
A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.
Want to see the full answer?
Check out a sample textbook solutionChapter 3 Solutions
Biochemistry
- Give two advantages and two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nmarrow_forwardQualitative Analysis of Proteins 1. Fill out the table below by providing the necessary information indicated per column. 2. As you have virtually conducted these qualitative tests for proteins, what do you think could be the essential practical or real-life applications of these tests?arrow_forwardChoice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).arrow_forward
- Titration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.arrow_forwardNonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?arrow_forward(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.arrow_forward
- Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3.arrow_forwarda. 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? Explainarrow_forwardWhy different amino acids have different Rf values? If you separate a mixture of amino acids consist of glutamic acid, histidine, glycine, tryptophan and isoleucine with paper chromatography using NH3: Benzene (10:90) as a mobile phase what do you expect the Rf values of the amino acids will be?arrow_forward
- NOTE: PLEASE SEND A CLEARER IMAGE PLEASE 1. Ionization scheme of Phenylalanine, methionine, tyrosine, and asparagine are shown below: (Acidic to basic form in the pH) NOTE: PLEASE SEND A CLEARER IMAGE PLEASEarrow_forwardIdentification. Write in CAPITAL LETTERS. Wrong spelling, wrong. Proteins are classified according to function,examples of these classes are: _____________________, ________________________, ____________________________, ______________________________, ____________________________, ___________________________, _____________________________.arrow_forwardPRECIPITATION OF PROTEINS What are peptides? Do all proteins possess peptide bonds? Do all proteins respond to Biuret’s test? What is the difference between coagulation and denaturation? Why is egg white used as an antidote for lead and mercurial poisoning? Explain its mechanism of action. 4.Why is silver nitrate used in the cauterization of wound? Explain your answer.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON