Which of the following accurately describes the method of ion-exchange chromatography? more than one option are correct increasing the salt concentration of the mobile phase can disrupt noncovalent interactions between proteins bound to the ion-exchange resin proteins are covalently bound to the stationary phase until salt elutes them from the column. a covalent bond between a charged functional group and the resin prevents the O functional group from eluting from the column when the salt concentration is increased
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- Under what pH conditions can a protein not bind to the beads in a column? pH = -pKa pH = pI pH = 7 pH = pKa In size exclusion/gel filtration chromatography, the elution order is dependent upon Molecular weight Concentration Overall Charge Enzymatic Activityat punctures the bacterial cell wall has just been recently isolated from the F the peptide reveals the following information below: IOTE: when the sequence is nat knawn, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 °C Heptapeptide (2) Arg, Pro, Phe, Tyr, Ala, Lys 2.4-dinitrofluorobenzene DNP-Phe Lys and modified free Peptide 1 (Ala, Lys) amino acids Cleovoge with Trypsin, then chromatography Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Cleavage with Chymotrypsin, then chromatography Peptide 4 (Arg, Tyr) Peptide 5 (Lys, Pro, Ala, Arg) When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter. 1. What is the C-terminal residue? K 2. What is the N-terminal residue? F 3. What is the sequence of Peptide 3? GP 4. What is the sequence of Peptide 5? LPAA 5. What is the averall amino acid sequence? AL100ml of LB media with 25 μg/ml of Amp and 100 μg/ml of Kan final concentration. You have 100ml of LB provided and Amp and Kan stocks at 100 mg/ml and 50 mg/ml provided. Determine how much of each antibiotic stock solution you need to add to 100ml of LB to reach desired antibiotic concentration.
- Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, Ion exchange chromatography is conducted via a software using DEAE-cellulose and method of elution is done by salt gradient. pH is set to 7. In terms of Molar, start of gradient is 0 and end of gradient is 1. The following graph is generated. Using the graph and analytical methods, determine pI of protein.Gel Running Buffer is made and kept at 14X concentration for storage. We will need 1.5 L of this solution at a concentration of 1X to run our gels. How would we make this solution? I am having trouble understanding the steps to this question, if you could please help me understand it that would be greatly appreciated!When combining 1ml of lysosome solution with a concentration of 5mg/ml and 1ml of water what is the final concentration of the lysosome solution after adding 8.0 of a biuret reagent to the solution 2.5mg/ml 1mg/ml 0.5mg/ml 5 mg/ml
- Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.A purified protein is in a Hepes (N-(2-hydroxy-ethyl)piperazine-N′-(2-ethanesulfonic acid)) buffer at pH 7 with 500 mM NaCl. A sample (1 mL) of the protein solution is placed in a tube made of dialysis membrane and dialyzed against 1 L of the same Hepes buffer with 0 mM NaCl. Small molecules and ions (such as Na+, Cl+, and Hepes) can diffuse across the dialysis membrane, but the protein cannot.(a) Once the dialysis has come to equilibrium, what is the concentration of NaCl in the protein sample? Assume no volume changes occur in the sample during the dialysis.(b) If the original 1 mL sample were dialyzed twice, successively, against 100 mL of the same Hepes buffer with 0 mM NaCl, what would be the final NaCl concentration in the sample?A biochemist wants to separate two peptides by ion-exchange chromatography. At the pH of the mobile phase to be used on the column,one peptide (A) has a net charge of −3 due to the presence of more Glu andAsp residues than Arg, Lys, and His residues. Peptide B has a net charge of+1. Which peptide would elute first from a cation-exchange resin? Whichwould elute first from an anion-exchange resin?
- A mixture of dipeptides consisting of Lys-Gly, Thr-His, Ser-Leu, Glu-Gln was applied to column packed with cation-exchange resin at pH 6.0. Which of these dipeptides would be eluted from the column first? O Lys-Gly first O Thr-His first O Ser-Leu first O Glu-Gln first OA mixture of Thr-His and Ser-Leu first2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants? Size exclusion column Ion exchange column Affinity chromatography using glucose as the bait Affinity chromatography using NAD as the bait Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.A purified protein is in a HEPES (N-(2-hydroxyethyl)piperazine-N-(2-ethanesulfonic acid)) buffer at pH 7 with 600 mM NaCl. A 1 mL sample of the protein solution is placed in a tube made of dialysis membrane and dialyzed against 2.0 L of the same HEPES buffer with 0 mM NaCl. Small molecules and ions, such as Na, Cl, and HEPES, can diffuse across the dialysis membrane, but the protein cannot. Once the dialysis has come to equilibrium, what is the concentration of NaCl in the protein sample? Assume no volume changes occur in the sample during the dialysis. [NACI] = mM If the original 1 mL sample were dialyzed twice, successively, against 100 mL of the same HEPES buffer with O mM NaCl, what would be the final NaCl concentration in the sample? [NaCl] = mM