26 To determine the number of disulfide bridges in a protein molecule one has toa. Treat the protein with reducing gent then titrate the SH groups.O b. Titrate the protein SH groups before and after treating it with detergentsOc.Determine the protein SH groups before and after treating it with reducing agentd.Treat the protein with an oxidizing agent to unfold the protein then titrate thenumber of SH groups

Cysteine is an amino acid with a terminal thiol group (-SH) in its sidechain. A disulfide bridge is…

Answered: To determine the number of disulfide…

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
What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weight
Proteins can be precipitated out of aqueous solution bythe addition of an electrolyte; this process is called “saltingout” the protein. (a) Do you think that all proteins wouldbe precipitated out to the same extent by the same concentrationof the same electrolyte? (b) If a protein has beensalted out, are the protein–protein interactions stronger orweaker than they were before the electrolyte was added?
Which of the following statements best describe(s) the mechanism by which correct protein folding takes place once the misfolded protein binds the open ring of groEL? Select all that apply. The groEL ring closes to isolate the protein and provide enough time for the protein to properly fold on its own. b and d The groEL ring closes to provide a hydrophilic space to isolate the protein and inhibit its aggregation with others until properly folded. The groEL ring closes to isolate the protein and provide steric hindrance that mechanically refolds the protein. The groEL ring closes to isolate the protein and decode the information necessary to achieve the correct three-dimensional structure. None of the above I picked "The groEL ring closes to provide a hydrophilic space..." but it was incorrect..
first amino acid is R second amino acid is L Draw your dipeptide at pH 7.4 What is the Log Kow of the pesticide What is the molar concentration in the octanol phase What is the number for the pesticide How many chiral centers does your assigned pesticide contain?
When a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
Tertiary structure of protein is maintained by Select one: a. Hydrogen bond b. All of these c. Di-sulphide bond d. Peptide bond
This image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.
Which of the following is true regarding proteins A. Absorbance of proteins is directly proportional to the molecular weights B.Proteins react with biuret reagent because of their side chains C. two out of the twenty amino acids can absorb at 280nm D. In proteins the average weight per amino acid residue always varies
Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactions
You are purifying a protein for the first me and decide to analyze it on SDS PAGE. You run two lanes on the gel, one with DTT and one without DTT (DTT is a subs tute for Beta-mercaptoethanol that is less s nky) The lane with DTT yields 2 bands one at 30kD and one at 20kD while the one without yields a single band at approximately 50 kD. A. What does this result suggest about the overall protein structure?B. Sketch what may be occurring in this protein natively.
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