Question 6.The solubility of globular proteins, when dissolved in water, is influenced by the factors/conditions listedbelow. Describe how these conditions would affect the solubility of the protein:a. pH of the buffer is the same as the pl of the proteinb. the pH of the solution is 12c. the solution is heated to 100°Cd. the solution contains 0.01 M NaCIc. the solution contains 70% ammonium sulphatef. the protein is dissolved in a 75% cthanol solutiong. urea is added to the solutionh. What does urea do to the protein structure?i. mercapto-ethanol is added to the solution

Globular proteins are the folded proteins that consists of hydrophilic aminoacids on the surface and…

Answered: Question 6. The solubility of globular…

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

QUESTION 3 An unknown protein was determined using the following method: Bradford method Reagents Stock Bradford reagent: Dissolve 100 mg Coomassie Brilliant Blue G250 in a mixture consisting of 100ml of 85% phosphoric acid, 50ml of 95% ethanol and 50ml 1M NaOH. Store at 4°C until precipitation occurs, at which point it is discarded. Working Bradford reagent: Prepare fresh by diluting 10ml of stock Bradford reagent to 250ml with distilled water. Stock bovine serum albumin (BSA) solution (10mg/ml): Dissolve 0.2g BSA in 20ml distilled water. Working BSA concentration range: 0.5 – 1.25 mg/ml Method 1. Prepare the following test tubes: Table 1: Preparation of test tubes for the Bradford method Blank Tube 1 Tube 2 Tube 3 Tube 4 Tube 5 Unknown Distilled H20 1.0 ml 0.9ml 0.9ml 0.9ml 0.9ml 0.9ml 0.8ml 0.25 mg/ml BSA 0.1 ml 0.5 mg/ml BSA 0.1 ml 0.75 mg/ml BSA 0.1 ml 1.0 mg/ml BSA 0.1 ml 1.25 mg/ml BSA 0.1ml Unknown 0.2ml protein Working 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml Bradford 2.…
To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?
A large chaperone protein complex GroEL is approximately 16 nm in diameter. When it is dissolved in water at 300 K, estimate the average time it will take for GroEL to diffuse a distance of 500 nm (0.5 micron). The viscosity of water is 10-3 Pa*s.
2. 0.1 mL of a protein solution of concentration of 7 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). 3 mL of this solution was then mixed with 27 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex
16. A quantitative study of the interaction of a protein with its ligand yielded the following results: Ligand concentration 0.5 1 2 3 4 5 6 9. 12 (μM) v (moles of 0.14 0.31 0.48 0.61 0.68 0.72 0.77 0.79 0.81 ligand bound per mole of protein) Plot a graph of ligand concentration versus v. Determine KD, the dissociation constant for the interaction between the protein and its ligand, from the graph.
A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
The following data is protein melting point (Tm) characterization data obtained by the Zetasizer Nano System (Dynamic Light Scattering method, DLS)². The melting point for the series of proteins are measured in PBS (phosphate buffered saline). Which protein is structurally the most stable form in PBS? State your reasoning in full sentence. Z average in DLS: The dynamic size of particle. * 100 Protein T.(°C) 38 65 71 64 68 90 Bovine Hemoglobin Bovine Serum Albumin Ovalbumin Human Insulin Hen Egg Lysozyme 80 70 60 50 40 30 20 10 30 35 40 45 50 55 60 65 70 75 80 Temperature (°C) Z Average Diameter (nm)
When performing a separation by ion-exchange chromatography, the rate of elution of an amino acid is influenced by three main factors: a. Temperature b. Solution (buffer) pH c. Ionic strength (buffer concentration) of the eluent Briefly, explain how each of these parameters influences elution rate. Please provide only typed answer solution no handwritten solution needed allowed
10. Match each chromatographic method with the characteristics of the protein that you would expect to find in the flow-through or in early fractions. Provide number to right. a. Cation-exchange chromatography b. Anion-exchange chromatography c. Size-exclusion chromatography d. Hydrophobic interaction chromatography e. Immobilized metal ion affinity chromatography (IMAC) Possible answers: 1. Negatively-charged proteins 2. Positively-charged proteins 3. High molecular weight proteins 4. Hydrophilic proteins 5. Untagged proteins 6. Hydrophobic proteins 7. Low molecular weight proteins 8. 6x-His tagged proteins
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…
You are super jazzed because your protein is purified and at a concentration of 600 μg in 1.75 ml of buffer. Convert this concentration to mM. Note that biochemisfunase has a molecular weight of 54,321 Daltons (which is just another unit for g/mol). Show your calculations.

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