10. Match each chromatographic method with the characteristics of the protein that you wouldexpect to find in the flow-through or in early fractions. Provide number to right.a. Cation-exchange chromatographyb. Anion-exchange chromatographyc. Size-exclusion chromatographyd. Hydrophobic interaction chromatographye. Immobilized metal ion affinity chromatography (IMAC)Possible answers:1. Negatively-charged proteins2. Positively-charged proteins3. High molecular weight proteins4. Hydrophilic proteins5. Untagged proteins6. Hydrophobic proteins7. Low molecular weight proteins8. 6x-His tagged proteins

Introduction: Chromatography is an analytical technique in which compounds in a mixture are…

Answered: 10. Match each chromatographic method…

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 elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography
A mixture of two proteins (both with mass of 50 kDa) with an molecular isoelectric points of 7.8 and 8.9, respectively, is in a buffered solution at pH 7. Which type of liquid chromatography would be used to separate these two proteins? O a. O b. O C. d. e. anion exchange chromatography size-exclusion column gel filtration Ni-NTA column cation exchange chromatography
You run 5 standard proteins listed below on a size-exclusion (gel filtration) column with limit of 200,000Da. Please draw a chromatogram on a separate page with each peak and both axes labeled. Protein B-Amylase Alcohol dehydrogenase Bovine albumin Carbonic anhydrase Cytochome A280 MW 223,800 0.5 82,000 0.6 66,463 0.45 30,000 0.43 12,000 0.8
I am not understanding why TA of alcohol precipitation is used as TA of purified protein. I provided 2 photos, 1 with the questions and the correct answer, and the other photo is a screenshot of the explanation.
PLEASE have the following and help D:. What i need for the chosen of 2/3 choices. 2) Illustrate detailed chemical scheme for how you will functionalize your biomolecule to the surface of the sensor (e.g. if you wanted to functionalize a protein to a gold SPR chip, you should could show the assembly of an amine-terminated SAM, followed by carbodiimide coupling of. the protein). These schemes should be drawn using a chemical illustration software package (ChemDraw / ChemSketch).Your chemical schemes should be as detailed as necessary to accurately depict the chemical design of your system, DO NOT INCLUDE a step-wise mechanism, it is not necessary. You should include at least one literature reference to support your conjugation strategy.3) Include an illustration of the functional sensor, and describe whether the sensor is label-free or not, what signal is observed, and how you would detect the interaction (i.e. if a labeled antibody is required, you should describe what label would…
Sucrose + H2O(negative control): Colorless to brown solution: Blue solution Conclusion for Iodine test A. amylose present B. amylose not present Conclusion for Benedict's test A. reducing sugars not present B. reducing sugars present Sucrose + HCl(potential hydrolysis): unchanged compared to sucrose+water: Conclusion for Iodine test A. more amylose present B. LESS amylose present C. NO change Conclusion for Benedict's test a. more reducing sugar present b. less reducing sugar present c. no change Did hydrolysis of sucrose occur in the presence of acid? A. Yes B. no
You are analyzing the peptide ala-ile-glu-lys-phe-val- tyr-cys. If you treat the peptide with chymotrypsin, which technique would be best to separate the fragments? O a. ultracentrifugation O b. affinity chromatography O c. dialysis d. gel filtration chromatography O e. ion exchange chromatography What is an advantage of NMR spectroscopy over x-ray crystallography in studying protein structure?
A purified protein fraction has a total sample volume of 360 µL. The sample has a corrected A280 of 0.484, and the blank corrected A280 was 0.052. (Both values were measured with a path length of 1.00 cm.) If 5.00 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).
Which of the following statements concerning SDS in SDS-PAGE is INCORRECT? a. SDS is a negatively charged detergent b. SDS can give all proteins a uniform charge c. the full name of SDS is sodium dodecyl sulfate d. SDS make protein gel electrophoresis to separate proteins based on molecular weight as well as protein surface charges e. SDS can denature proteins

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