2. 0.1 mL of a protein solution of concentration of 7 mg/mL was diluted to a total volume of 4.0 mLwith water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 3 mL of this solution wasthen mixed with 27 mL of water.What is the concentration of the diluted protein solution?Space to show your workings:

The c1v1 formula is a mathematical expression that is used to calculate the relationship between the…

Answered: 2. 0.1 mL of a protein solution of…

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

Solution A contains 100 mmol/L glucose and Solution B contains 50 mmol/L NaCl. Assume that gNaCl is 2.0, σglucose is 0.5, and σNaCl is 0.8. If a semipermeable membrane separates the two solutions, what is the direction of water flow across the membrane?
A solution of Na2CO3 contains 53g of solute in 200ml of solution. What is the molarity of this solution.
Protein A is made up of a single polypeptide chain; The molecular mass of A is 20,000 Da; the A molecule has 2 tryptophan residues, 5 tyrosine residues, and no disulfide bonds. Calculate what absorbance (at 280 nm) a solution of protein A will have at a concentration of 1.0 mg / mL, in a 1 cm cell. Write the calculations you have done.
Protein Solubility 3.5 5 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 pH 15 7.5 1.5 4.5 5 0.027 3 0.042 5.5 5 0.068 0.130 Protein Solubility Versus pH 6 6.5 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 Please provide a brief discussion and explanation of the results. 7.5 7.5 50 0.032 0.053 9 8.5 50 0.054 0.100 21.429%
A mixture of Alanine (pl 6.02), Glutamic Acid (pl 3.22), Glycine (pl 5.79), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2 ? v First 1. Alanine v Second 2. Glutamic Acid v Third 3. Glycine v Fourth 4. Lysine v Fifth 5. Threonine 6. No separation
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, size exclusion chromatography is being done. Use the graph below and analytical methods to determine molecular weight of protein.
We have isolated a mixture of 2 protein of the same molecular weight but different isoelectric points. The isoelectric points are 7.5 for Protein A and 9.0 for Protein B. What would be the order of elution from a cation exchange column if a buffer of pH 7 is used? Group of answer choices Both proteins will remain in the column. Both proteins will elute simultaneously Protein B followed by Protein A Protein A followed by Protein B
Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.
Molar concentration 1.0 Molar concentration Depicted below is a cell membrane separating two closed compartments, each filled with one liter of H₂. You add one mole of each of the molecules as shown below. The molecule to which the membrane is most permeable diffuses across at a net rate of 0.5 moles/hour. Based on this information, answer the following questions. 1.0 0₂ Nat 0.5- fructose glycerol K+ 2. Graph the expected relative concentrations of each solute in the right hand compartment as a function of time. 1 Time in hours Nat 1. Immediately after adding these solutes, will there be a net movement of H₂O molecules across the membrane in one direction? If so, in which direction and why? through right K+ 3. Finally, you add ATP to the left side compartment at the time indicated by the arrow below, and measure concentration of Nat and K+ in the right side compartment. Your results are graphed below. Propose a hypothesis to explain the results you obtained in this experiment. 2 (10…
You have an aqueous solution of hemoglobin (pl = 6.8) at pH 5.2, and currently the proteins are soluble. If you had 1M HCl and 1M NaOH at your disposal, what could you do to precipitate the albumin out of solution? add NaOH to the solution O add HCl to the solution O add NaOH to the solution, then add equal volume of HCl to the solution O add HCl to the solution, then add equal volume of NaOH to the solution
number 57.) what's the answer
Given this: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340 Y-globulin 6.6 160 Collagen 6.6 115 Hemoglobin (monomer) 7.1 16 Мyoglobin 7.0 16.7 What is the appearance after visualization of a protein mixture containing the seven proteins above when subjected to SDS-PAGE?

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