A set of biomolecules listed in the table at right are insolution at pH 6.8, when they are passed through the multi-stepseparation process shown below. The sample passes through anultrafilter with MWCO of 50,000 (assume this filter gives aperfect separation of molecules above and below the MWCO),and the retentate then flows through an ion exchange columnfilled with beads that have a positive charge under the operatingconditions (pks = 7.3).InletBiomolecule MixturepH 6.8UltrafiltrationMWCO 50,000PermeateRetentatelonExchangeColumnBiomolecule Molecular weight plA68,0004.2B92,6009.6C144,000A-3. Which biomolecules (A, B, C, etc.) exit the process in the permeate stream?KC-3. Which biomolecules are retained inside the ion exchange column?DEFGHB-3. Which biomolecules exit the process after passing through the ion exchange column?5,80068,000Packed withDEAE cellulosebeads, which havepositively chargedgroups below a pH of7.3156,00045,00016,000None (nocharges)5.35.08.15533s3.57.6

Ultrafiltration is a technique similar to dialysis where the sample containing a mixture of proteins…

Answered: A set of biomolecules listed in the…

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

See similar textbooks

Similar questions

The molecular iodine (12) in betadine is susceptible to decomposition if exposed to direct sunlight, which lowers the concentration of 12 solution. After performing the standardization step in home experiment 9, a student leaves their betadine solution in direct sunlight for several hours before coming back to perform the titration of ascorbic acid in orange juice. Assuming that the concentration of 12 is reduced by the sunlight, how would this affect the measured value of the concentration of ascorbic acid in the orange juice? The measured concentration of ascorbic acid would be higher The measured concentration of ascorbic acid would be lower There is not enough information to determine the affect on the measured concentration of ascorbic acid The measured concentration of ascorbic acid would be unaffected
(please type answer with explanation).
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).
Phosphate buffers are commonly used to mimic biological systems. Given that phosophoric acid is a triprotic acid with three pKas (2.12, 7.21, and 12.32), why do you think this is? What are the dominant buffering compounds present in a phosphate buffer near physiological pH?
What is the predominant ionic form of ribose-5-phosphate at physiological pH? Would ribose-5-phosphate be a good biological buffer for cells?
Polymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
Laemmli buffer, also referred to as SDS-reducing buffer, is added to each of the samples. It is a blue solution and the recipe for 2X Laemmli buffer is: 0.125 M Tris HCl, pH 6.8, 20% glycerol, 4% SDS and 10% β-mercaptoethanol (βME). What is the purpose of each of these ingredients?
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS