Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 3, Problem 23P
Interpretation Introduction
Interpretation:
The cause of the difference between the predicted and the observed masses of a fragment of the peptide from a protein should be determined. Also, the origin of this fragment should be determined.
Concept introduction:
A peptide bond is present between the two amino acids in a protein. During the formation of a peptide bond, a molecule of water is released. The amino group of an amino acid gets associated with the carboxyl group of another. Polypeptides and proteins are the chains formed by the amino acids.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Please help! Sketch a titration curve of the peptide Ala-Tyr-Gln-Met-Asp-His from pH=0 to 14 up to 5 equivalnets of KOH
(Please type answer)
Affinity chromatography
You have created a fusion protein tagged with Glutathione-S-Transferase (GST). Your lab mate tells you that the affinity columns for this type of tagged protein are very similar to that of Histadine tagged proteins.
Using the following elements set up a purification column and construct a protocol for an affinity purification using this tag.
A large amount of glutathione is usually used to elute the tagged protein off the column. How might this work?
Shape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?
Chapter 3 Solutions
Biochemistry
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
Knowledge Booster
Similar questions
- Help? Please explain salting out in protein purification.arrow_forwardSedimenting spheres. What is the dependence of the sedimentation coefficient s of a spherical protein on its mass?How much more rapidly does an 80 -kDa protein sedimentthan does a 40-kDa protein?arrow_forwardPurification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…arrow_forward
- Ionization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?arrow_forwardPlease help me with this question. How many amino acid residues are in the heavy and light chains of the Fab fragment, and how many amino acid residues are in lysozyme?arrow_forwardPro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.arrow_forward
- In Multi-Column Purification of rGFP. What happens to the protein amount, protein purity, and/or specific activity of a purification fraction if one of the three is changed? (i.e. understand the relationship between the three.)arrow_forwardBased. On the table explain the difference of net charge between 168.1 and the 168.10 molecular clones. Consider the initial net charge of the 168.1 clone and what ionizable amino acids contribute to such charge. Assume that histidine is neutral due to the pharrow_forwardCENTRAL DOGMA & STRUCTURE-FUNCTION RELATIONSHIPS IN PROTEINS You are a bacteriologist studying a pathogenic protein (the "BAD" protein) that contributes to diseases caused by Staphylococcus aureus. BAD functions as an aß heterodimer, and the a subunit (25kD) and ß subunit (75KD) are held together by an electrostatic interaction between K in the a subunit and D in the B subunit. You are trying to dissociate the BAD subunits to prevent pathogenesis in the bacteria. Which mutation would you make to prevent the BAD subunits from forming a dimer? Assume neutral pH. (A) introduce AAA → AGA point mutation in the a subunit gene (B) introduce GAC → GAG point mutation in the ß subunit gene (C) introduce GAT → CGT point mutation in the ß subunit gene (D) introduce two point mutations: AAG → GTG in the a subunit gene & GAC → CTC in the B subunit gene (E) introduce two point mutations: AAA → TGC in the a subunit gene & GAT → TGT in the B subunit gene second base in codon A TGT Cys TGC Cys TTT Phe…arrow_forward
- Peptide sequence using 1-letter code for amino acids: EDLSMTCFRH What is the net charge of this peptide at pH 9? Use the pKa values from Table 4-1 from Voet, Voet and Pratt. -2 -1 O +1 +2arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.arrow_forwardSDS-AGE analysis of protein for subunit composition: A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography (gel filtration). When subjected to gel electrophoresis in the presence of SDS only and SDS plus 2-ME, the following pattern of SDS-PAGE is observed. MM - molecular standard proteins with known molecular weight (in kDa) as shown on the left of the gel are used to determine the size of unknown proteins. a) Determine the subunit composition of this protein (i.e., how many subunits are in its quaternary structure?). MM SDS SDS 2-ME kDa 180- 160- 100- 90- 60- 50-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