Kwon Soon-young was asked by his CHEM 160.1 lab instructor to determine the isoelectric pH of an unknown proteinsample which is said to be 20% histidine (pI = 7.59), 25% lysine (pI = 9.74), and 55% arginine (pI = 10.76). He plans toperform isoelectric precipitation in order to determine the IpH of the unknown protein sample. From the three buffersolutions below, at which particular buffer system do you think the unknown protein is most likely to precipitate? Explainyour reasoning.BUFFER SYSTEMcitrate bufferbicarbonate buffermethylamine-methylammonium chloride bufferpH3.157.4110.46

Proteins are composed of twenty standard amino acids attached together via peptide bonds. These…

Answered: Kwon Soon-young was asked by his CHEM…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Purification of a protein of unknown structure has been achieved. The natural protein has a molecular weight of 240,000, according to size-exclusion chromatography. Using a concentration of 6 M guanidine hydrochloride in the chromatography, a single peak can be identified as the molecular weight (MW) 60,000 of a protein. B-mercaptoethanol (BME) and guanidine hydrochloride (GHC) are used in tandem to produce proteins with mass masses of 34,000 and 26,000, respectively. The structure of this protein can be inferred from these facts.
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you
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When protein X is subjected to dimethylsuberimidate and SDS electrophoresis a 50 kDa band is seen; when the protein X is subjected to SDS electrophoresis without DMS, two bands of 20 kDa and 10 kDa are seen. How many different oligomeric structures of the native protein X are possible, being consistent with these observed results? one two three none of the above which is the answrr? and explain
In a 0.1 M lysine solution, what are the individual concentrations of the protonated C-terminus form of the amino acid versus the non- protonated at pH 4 (pKa = 2.16)
A two-dimensional gel electrophoresis of a protein preparation revealed the presence of five monomeric proteins with the following molecular weights and Isoelectric points: | (10 kDa, pl = 5.6), II (25 kDa, pl = 7.7), III (55 kDa, pl = 5.6), IV (150 kDa, pl = 9.1), V (200 kDa, pl = 8.2). Using native chromatographic conditions which preserve enzymatic activity, what would be the predicted elution order for the five proteins on a gel filtration chromatography column: O1, II, II, IV, V O II, III, I, IV and V OV, IV, III, II, I O IV, V, II, III and I I and III, II, V, IV
The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
A two-dimensional gel electrophoresis of a protein preparation revealed the presence of five monomeric proteins with the following molecular weights and Isoelectric points: I (10 kDa, pl = 5.6), II (25 kDa, pl = 7.7), III (55 kDa, pl = 5.6), IV (150 kDa, pl = 9.1), V (200 kDa, pl = 8.2). Using native chromatographic conditions which preserve enzymatic activity, what would be the predicted elution order for the five proteins on a gel filtration chromatography column: O1, II, II, IV, V O II, III, I, IV and V V, IV, III, II, I IV, V, II, III and I I and III, II, V, IV
In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.

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