XI. Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. Use a maximum of 5 sentences for each item below. ( 1. Ultracentrifugation vs salting out process 3. Gel electrophoresis and capillary electrophoresis 2. Affinity chromatography vs ion-exchange chromatography 4. Gel filtration chromatography and isoelectric precipitation

XI. Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. Use a maximum of 5 sentences for each item below. ( 1. Ultracentrifugation vs salting out process 3. Gel electrophoresis and capillary electrophoresis 2. Affinity chromatography vs ion-exchange chromatography 4. Gel filtration chromatography and isoelectric precipitation

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter26: Biomolecules: Amino Acids, Peptides, And Proteins

Section26.SE: Something Extra

Problem 50AP: The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in...

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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.
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.
. An Analytical Chemist is analyzing a protein sample analysis using a light scattering technique. If the formulation of the subject sample has included surfactants or salt additives, which of the following would adequately apply? . The additives would impact the ionic strength of the sample B. The impact of additives influence can be nullified when using a Light Scattering technique. C. The effect of formulation additives would impact the protein sample analysis, and should be considered as a factor when analyzing the protein aggregation using light scattering technique.
Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true.pls explain
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what is The method that would be BEST to use to monitor protein secondary structure during the titration of a denaturing agent?
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.
A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
The -helical parts of myoglobin and other proteins stop whenever a proline residue is encountered in the chain. Why is proline never present in a protein helix?
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.)
In HPLC, why is purging being done before analysis of samples. Outline the procedure on how purging is performed.
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