"A protein has a pI point which can be used to separate proteins using ion exchange. If you have an anion exchange column and access to buffers of any pH, how could you isolate a protein with a pI of 7 from a mixture of proteins which also has proteins with pI points of 3 and 5" Write a few sentences or draw a picture.

"A protein has a pI point which can be used to separate proteins using ion exchange. If you have an anion exchange column and access to buffers of any pH, how could you isolate a protein with a pI of 7 from a mixture of proteins which also has proteins with pI points of 3 and 5" Write a few sentences or draw a picture.

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.45P: 22-45 Proteins are least soluble at their isoelectric points. What would happen to a protein...

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22-45 Proteins are least soluble at their isoelectric points. What would happen to a protein precipitated at its isoelectric point if a few drops of dilute HCl were added?
At the isoelectric point of a protein (select all that apply).SELECT ALL THAT APPLY a. the charge on the protein will be neutral. b. the protein molecules coagulate and precipitate from solution c. the pH of the solution will ways be less than 7. d. the pH of the solution will always be greater than 7. e. the pH of the solution will always be exactly 7.
Write down the structure of glutamic acid in each pH range from acidic to basic. It is known that pKa1 = 2.5 pKa2 = 3.5 pKa3 = 8.7 and draw the titration curve of glutamic acid titrated with a strong base, such as NaOH.
How would you make 2.0 L of electrotransfer buffer for transferring the proteins from a gel onto nitrocellulose? Its composition is the following in water: 25 mM Tris (this is a solid; MW = 121) 192 mM Glycine (this is a solid; MW = 75.07) 20.0 % Methanol (you have 100% from the stockroom)
what is the role of Cu+2 ion in biuret test for proteins?
The denaturing of proteins occurs when the stabilizing forces are altered. Below is the set of processes in which proteins are denatured. Classify the following processes according to the denaturing agent involved. Please help me understand the diff and correct any mistakes.
What does high NaCl do to protein that is bound to a Sp column?
a) 75mL of a 0.2M solution of a tripeptide Ser-Cys-His is adjusted to pH=8.6. The solution is then titrated with 50mL of 0.5M HCl. Calculate the new pH value of the tripeptide solution. (Relevant pKa values are: 2.2, 6.0, 8.3, and 9.6). b) Once you've completed the addition of HCl to the tripeptide in part a you then titrate the solution with 30 mL of 0.6M NaOH. Calculate the final pH value of the tripeptide solution.
A solution with 5 mg/mL of a colored protein has an absorbance of 0.250. What is the concentration of a sample of that protein whose absorbance is 0.90?
You are supplied with the following: NaCl (Mr = 58.443 g/mol) 2.5 M Tris-Cl, pH 8 oplossing / solution (1 Litre) EDTA, sodium salt (Mr = 380.2 g/mol) 10 % Sodium dodecyl sulfate solution Proteinase K solution (50 mg dissolved in 1 ml ddH2O) You need a digestion buffer consisting of the following: 15 mM NaCl 75 mM Tris-Cl, pH 8 16 mM EDTA, pH 8 0.8 % Sodium dodecyl sulfate 0.75 mg/ml proteinase K Calculate: How will you prepare 500 ml of the digestion buffer? Show all your steps and calculations and remember to explain how exactly you will make it up.
Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions? How many grams of the protein are in one 200 g glass of milk?
Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intracellular abundance. Describe a quantitative approach to determine the number of molecules of an enzyme per cell.