BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 3, Problem 14P
Interpretation Introduction
Interpretation:
The strategy to develop a suitable assay for an enzyme showing a catalyzed reaction 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 solutionStudents have asked these similar questions
SIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met).
Polymerase with H2N-...GMMTVPPKKKRVGMMTV...-COOH
Provide the amino acid sequence of the signal peptide
Where will this polypeptide be transported?
What is the receptor of the signal sequence?
What is the transport complex for this protein?
Inducers and Inhibitors of AEP.
Short peptides such as legumain stabilization and activity modulation (LSAM) domain and αvβ3 integrin could enhance the activity of AEP. LSAM domain known as the prodomain of AEP blocks substrate binding before activation. This prodomain has a helical structure and two independent peptides. One is an activation peptide (AP, K287 to N323), and the other is a LSAM domain. LSAM domain remains even after AP is cleaved and released from protease at neutral pH via electrostatic interaction. AEP without LSAM domain has a lower melting temperature than AEP with LSAM domain [77, 117]. Another short peptide, αvβ3 integrin, can directly interact with AEP, and after forming a complex, the optimal pH for AEP activity is increased from 5.5 to 6.0. It indicates that αvβ3 binding could induce conformational stabilization of AEP accompanied by deprotonated C189. αvβ3 does not directly interact with the AEP active site; however, AEP docks to the αvβ3 RGD-binding site…
TPA protein function. Use at least two sentences to describe the function of the TPA protein.
Chapter 3 Solutions
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
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
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
- 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_forwardDo not give handwriting solution.arrow_forwardproteins. Which of the following will tell you whether a protein would be found in the lumen of the ER? A. You run a hydropathy plot an look for hydrophobic peaks that span 20-30 amino acids B. You isolate microsomes and see whether the proteins are inserted into the membrane of the microsome C. You run a hydropathy plot an look for a lack of hydrophobic peaks that span 20-30 amino acids O D. You do in vitro translation of each protein in the presence or absence of microsomes and look to see whether there is a size change in the presence of microsomes.arrow_forward
- LACTOSE .how will you inoculate? .How will you incubate? . what are Post- Incubation procedures? . How will you read the positive and negative results?arrow_forwardTrue or False. Explain. A) At no time during protein synthesis does an amino acid make direct contact with the mRNA being translated. B) Because the two strands of DNA are complementary, the mRNA of a gene can be synthesized using either strand as a template.arrow_forwardCold-Reacting Autoantibodies. Most adult sera contain low titers of cold-reacting autoantibodies, most notably autoanti-I, autoanti-H, and autoanti-IH. These antibodies are usually IgM and of no clinical significance. They are troublesome in that they may interfere with the detection of significant antibodies, resulting in prolonged workups and delayed transfusions.Cold-reacting autoantibodies may be suspected when the screen cells, panel cells, and the autocontrol areall positive at the immediate spin phase and reactivity gets weaker or disappears with incubation at 37°C (Fig. 9–18).Certain cold autoantibodies activate complement and may be detected at the AHG phase when using complement-containing AHG reagent. These autoanti- bodies may be mistaken for weakly reacting IgG antibodies.Although it is not usually necessary to determine the specificity of the cold autoantibody, testing against additional cells may confirm its presence. Cord blood cells that lack the I antigen are of…arrow_forward
- SIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Protease with mannose-6-phosphate Where is the receptor for this protein located? Where is the final destination of this polypeptide? What happens to the receptor after protein transport?arrow_forwardJustify. Peripheral protein is easiest to isolate and study.arrow_forwardTrue or false .Very powerful X-rays used in crystallography are generated in a very large facilities called synchrotron .A western blot allows detection of proteins after SDS-PAGE with higher sensitivit .Keratin and collagen adopt helical structures whereas silk fibroin adopts beta sheet structures .arrow_forward
- Need help, please.arrow_forwardThank you. The expert seems made a typo. The correct answer should be "(f) sample B has more Ras protein", instead of (d).arrow_forwardLeaderless. The MRNA for the A repressor begins with 5'-AUG-3', 5'-AUG-3', which encodes the methionine residue that begins the protein. What is unusual about this beginning? Would it cause the MRNA to translate efficiently or not?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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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