Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 5, Problem 2E
Summary Introduction
To explain: The ways to link the two polypeptide chains of protein through the disulfide bonds that was denatured by mercaptoethanol.
Concept introduction: Disulfide bonds play a vital role in folding and maintaining the stability of proteins. To explore the protein structure, it is important to break the disulfide bond. Mercaptoethanol is the chemical compound mainly used to reduce the disulfide bonds in proteins and to protect the sulfhydryl groups from oxidation. There are two side chains in the mercaptoethanol with the molecular weight of 40kD and 60kD, respectively.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
a) What are the differences between the Direct & Indirect Immunofluorescence Assays? (0.5 mark)
b) What are the advantages of the Indirect Immunofluorescence Assays? (0.5 mark)
c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality? (2 marks)
a) What are the differences between the Direct & Indirect Immunofluorescence Assays?
b) What are the advantages of the Indirect Immunofluorescence Assays?
c) A Super-Resolution Imaging Technique was developed in 2018 using imidazole, a His-tag ligand conjugated with a fluorophore to report the presence of a recombinant His-tag protein target, (Sci Rep, 2018, 8:5507). How does this technique improve the image quality?
Calculate the number of ATP produced from oxidation of 1 molecule of glucose
Chapter 5 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 5 - Prob. 1ECh. 5 - Prob. 2ECh. 5 - 3. Which peptide has greater absorbance at 280...Ch. 5 - 4. Protein X has an absorptivity of 0.4 mL · mg?1...Ch. 5 - 5. You are using ammonium sulfate to purify...Ch. 5 - Prob. 6ECh. 5 - 7. (a) In what order would the amino acids Arg,...Ch. 5 - Prob. 8ECh. 5 - 9. Explain why a certain protein has an apparent...Ch. 5 - 10. Determine the subunit composition of a protein...
Ch. 5 - 11. Explain why a protein, which has a...Ch. 5 - 12. A protein has an apparent mass of 800 kD by...Ch. 5 - 13. Explain why the dansyl chloride treatment of a...Ch. 5 - 14. Identify the tint residue obtained by Edman...Ch. 5 - 15. A pentapeptide has the sequence NNKNN (using...Ch. 5 - 16. The peptide in Problem 15 was sequenced by...Ch. 5 - 17. In site-directed mutagenesis experiments, Gly...Ch. 5 - 18. Below is a list of the first 10 residues of...Ch. 5 - Prob. 19ECh. 5 - Prob. 20ECh. 5 - Prob. 21CQCh. 5 - Prob. 22CQCh. 5 - 23. What fractionation procedure could be used to...Ch. 5 - Prob. 24CQCh. 5 - 25. Purification tables are often used to keep...Ch. 5 - Prob. 26CQCh. 5 - 27. You must cleave the following peptide into...Ch. 5 - 28. You wish to determine the sequence of a...Ch. 5 - Prob. 29CQCh. 5 - Prob. 30CQCh. 5 - 31. You wish to determine the sequence of a short...Ch. 5 - Prob. 32CQCh. 5 - Prob. 33CQCh. 5 - 34. You wish to sequence the light chain of a...Ch. 5 - Prob. 1MTE
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Example 1: 1. Suppose an enzyme (MW = 5,000 g/mole) has a concentration of 0.05 mg/L. If the kcat is 1 x 10 s, what is the theoretical maximum reaction velocity for the enzyme? A) 1050 µM/s. B) 100 µM/s. C) 150 μM/s. D) 105 μM/s.arrow_forwardIn 1956, E. P. Kennedy and S. B. Weiss published their study of membrane lipid phosphatidylcholine (lecithin) synthesis in rat liver. Their hypothesis was that phosphocholine joined with some cellular component to yield lecithin. In an earlier experiment, incubating 32 P-labeled phosphocholine at physiological temperature (37 °C) with broken cells from rat liver yielded labeled lecithin. This became their assay for the enzymes involved in lecithin synthesis. Determine the optimal pH for this enzyme and characterize the enzyme activity at different pH values. -O-P-O-CH2-CH₁₂-N(CH3)3 Phosphocholine H₂C-O-C-R HC-O-C-R2 + + + Cell fraction + ? HC-O-P-O-CH₁₂-CH₂-N(CH), O Phosphatidylcholine The researchers then centrifuged the broken cell preparation to separate the membranes from the soluble proteins. They tested three preparations: whole extract, membranes, and soluble proteins. Table 1 summarizes the results. Table 1: Cell fraction requirement for incorporation of 32p-phosphocholine into…arrow_forwardResearchers isolated an unknown substance, X, from rabbit muscle. They determined its structure from the following observations and experiments. (a) Qualitative analysis showed that X was composed entirely of C, H, and O. A weighed sample of X was completely oxidized and the H2O and CO2 produced were measured. This quantitative analysis revealed that X contained 40.00% C, 6.71% H, and 53.29% O by weight. (b) The molecular mass of X, as determined by mass spectrometry, was 90.00 atomic mass units (u). (c) Infrared spectroscopy showed that X contained one double bond. (d) X dissolved readily in water, and the solution demonstrated optical activity when tested in a polarimeter. (e) The aqueous solution of X is acidic. What is the empirical formula of X?arrow_forward
- Show work. don't give Ai generated solution....give correct solutionarrow_forwardBiochemistry What is the process of "transamination" in either the muscles or the liver, that involves keto acid or glutamic acid? Please explain how the steps work. Thank you!arrow_forwardBiochemistry Please help. Thank you What is the importance of glutamic acid in the metabolism of nitrogen from amino acids? (we know therole; it’s used to remove the nitrogen from amino acids so that the remaining carbon skeleton can bebroken down by the “usual” pathways, but what is the important, unique role that only glutamicacid/glutamate can do?)arrow_forward
- Biochemistry Please help. Thank you When carbamyl phosphate is joined to L-ornathine, where does the energy for the reaction come from?arrow_forwardBiochemistry Question Please help. Thank you What is the function of glutamate dehydrogenase?arrow_forwardBiochemistry Question Please help. Thank you How and why does a high protein diet affect the enzymes of the urea cycle?arrow_forward
- Biochemistry What is the importance of the glucose-alanine cycle?arrow_forwardBiochemistry Assuming 2.5 molecules of ATP per oxidation of NADH/(H+) and 1.5molecules of ATP per oxidation of FADH2, how many ATP are produced per molecule of pyruvate? Please help. Thank youarrow_forward1. How would you explain the term ‘good food’? 2. How would you define Nutrition? 3. Nutrients are generally categorised into two forms. Discuss.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
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
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
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