You have an aqueous solution of hemoglobin (pl = 6.8) at pH 6.5, and currently the proteins are soluble. If you had 1 M HCl and 1M NaOH at yourdisposal, what could you do to precipitate the albumin out of solution?O add NaOH to the solutionadd HCl to the solutionadd NaOH to the solution, then add equal volume of HCl to the solutionO add HCl to the solution, then add equal volume of NaOH to the solutionAn error has been detected in your answer. Check for typos,miscalculations etc. before submitting your answer.Submit AnswerTry Another Version1 item attempt remaining

pH affects the ionisation of amino acids and can thus influence the nature and distribution of…

Answered: You have an aqueous 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

Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?
1.0 ml of serum albumin (BSA) solution was precisely diluted to 100 ml with a buffer solution, and the absorbance at 280 nm was measured from this buffer solution at a distance of 1 cm from the light. The result was A=1.0. BSA is 0.1%(=0.1g/l). The absorptivity is e(0.1%)=0.667, so 1g/l solution gives an absorbance of 0.667. What was the original protein content? Report in the result unit mg/ml with an accuracy of 0.1 mg.
After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
You have given two proteins with a pI of 4.5 and pI of 7.7? Using an anion-exchange column, how can these two proteins be separated. What buffer could you prepare?
A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…
6 Concanavalin (ConA) is a 25.5KDa protein with pI of 4.7 and optical absorbance (A 0.1% 289) of 1.14. calculate the concentration of an aqueous solution of pure BSA protein with an absorbance of 0.66 at 280nm. give your answer in units of mg/ml ?
The molecular formula for glucose is C6H12O6. What would be the molecular formula for a polymer made by linking ten glucose molecules together by dehydration reactions? Group of answer choices A. C60H120O60 B. C60H102O51 C. C60H100O50 D. C60H111O51 Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers.…
You are given two proteins with a pI of 4.5 and pI of 7.7. In an example of an anion-exchange column, can you use a buffer to separate these two proteins? What buffer protein can be used to separate the two proteins mentioned above?
How many hemoglobin molecules are there in an average red cell? Assume that the molecular weight of the human hemoglobin tetramer is 65 kDa.
How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?
Normal Hgb is referred to as HbA and contains 4 subunits, 2 α-globin chains and 2 β-globin chains, arranged as two dimers of αβ. In Sickle Cell Disease, both β-globin chains are altered in the dimers (αβS/αβS). Q3: Which level of structure does the αβ/αβ and αβS/αβS in HbA and HbS describe?
if i have protein with 110kda and its cysteine joining with disulfide bond . and one cysteine acids per 100 amino when i heated at 85c it lost activity but if i cool it the activity will restore the questions are : how many disulfide bonds in this protein with explanation? and what is molecular basis to restore activity?

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