BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 31, Problem 32P
Interpretation Introduction
Interpretation:
The energy required during cotranslationaltransport of proteins across the ER membrane should be determined.
Concept introduction:
The transportation of secretory proteins having around 100 amino acids, into the lumen of ER, along with the ongoing translation process, is termed as the cotranslational transport. The proteins can be transported into the ER lumen by the help of a signal sequence, located at the N-terminal of the protein.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Please help me. Thank you.
TPA protein function. Use at least two sentences to describe the function of the TPA protein.
Leaderless. 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?
Chapter 31 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
Ch. 31 - Prob. 1PCh. 31 - Prob. 2PCh. 31 - Prob. 3PCh. 31 - Prob. 4PCh. 31 - Prob. 5PCh. 31 - Prob. 6PCh. 31 - Prob. 7PCh. 31 - Prob. 8PCh. 31 - Prob. 9PCh. 31 - Prob. 10P
Ch. 31 - Prob. 11PCh. 31 - Prob. 12PCh. 31 - Prob. 13PCh. 31 - Prob. 14PCh. 31 - Prob. 15PCh. 31 - Prob. 16PCh. 31 - Prob. 17PCh. 31 - Prob. 18PCh. 31 - Prob. 19PCh. 31 - Prob. 20PCh. 31 - Prob. 21PCh. 31 - Prob. 22PCh. 31 - Prob. 23PCh. 31 - Prob. 24PCh. 31 - Prob. 25PCh. 31 - Prob. 26PCh. 31 - Prob. 27PCh. 31 - Prob. 28PCh. 31 - Prob. 29PCh. 31 - Prob. 30PCh. 31 - Prob. 31PCh. 31 - Prob. 32PCh. 31 - Prob. 33PCh. 31 - Prob. 34PCh. 31 - Prob. 35PCh. 31 - Prob. 36PCh. 31 - Prob. 37PCh. 31 - Prob. 38PCh. 31 - Prob. 39PCh. 31 - Prob. 40PCh. 31 - Prob. 41PCh. 31 - Prob. 42PCh. 31 - Prob. 43PCh. 31 - Prob. 44PCh. 31 - Prob. 45PCh. 31 - Prob. 46PCh. 31 - Prob. 47PCh. 31 - Prob. 48PCh. 31 - Prob. 49PCh. 31 - Prob. 50PCh. 31 - Prob. 51PCh. 31 - Prob. 52P
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
- Biotransformation. Explain the process of enzyme induction. What are the benefits or down-falls of this process.arrow_forwardDo not give handwriting solution.arrow_forwardNeed help. (a) Two ligands bind to the same site of a protein. However, when examined by ITC, for one of the ligands heat needs to be added to the system to maintain constant temperature, whereas for the other ligand, heat must be removed. Why is this the case?arrow_forward
- need help.arrow_forwardPlease ASAP. Thank you.arrow_forwardQuestion 8 Review translation. Match the term and its description. Each term can only be used once. This site holds the tRNA that carries the growing polypeptide chain | Choose ) This site holds the tRNA that carries the next amino acid to be | Choose J added to the chain This site is the exit site, where discharged tRNAS leave the [ Choose ) ribosome Initiation, elongation and termination | Choose J >arrow_forward
- Need help. do explainarrow_forwardnerve impulses. Neurotransmitters are packaged by the cell into small, membrane- bound sacs called vesicles. Upon receiving a chemical signal, the vesicles move towards the cell membrane and fuse with it, releasing the enclosed neurotransmitters from the terminal end of the nerve cell. Which organelle is most likely responsible for packaging neurotransmitters into a vesicle? Mitochondria Golgi body Ribosomes Nucleusarrow_forwardDocking and Membrane Fusion. Q-8a. Choose from the terms below to Fill-in the Blanks. [All terms are used. Some terms are used more than once] Rab, SNARE, v- SNARE, t-SNARE, Tethering a. Identification of a vesicle to be docked depends on a diverse family of monomeric GTPases called proteins. First, a filamentous protein on a target membrane binds to a protein on the surface of a vesicle. This interaction allows the vesicle to dock on its particular target membrane. A on the vesicle then binds to a complementary_ on the target membrane. Whereas and proteins provide the initial recognition between a vesicle and its target membrane, complementary appropriate target membranes. Together, the proteins ensure that transport vesicles dock at their proteins catalyze the final fusion of the two membranes by squeezing out water making fusion more energetically favorable. b. What does the acronym SNARE stand for? c. Membrane fusion the rate limiting step of vesicular transport. Why? (What makes…arrow_forward
- Need help, please.arrow_forwardFrog poison. Batrachotoxin (BTX) is a steroidal alkaloid from the skin of Phyllobates terribilis, a poisonous Colombian frog (the source of the poison used on blowgun darts). In the presence of BTX, Na+Na* channels in an excised patch stay persistently open when the membrane is depolarized. They close when the membrane is repolarized. Which transition is blocked by BTX?arrow_forwardILLUSTRATIONS. For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. • Below your drawing, indicate: a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none A. Mitochondrion H₂N- MTS ITS* *Internal targeting sequence that has no cleavage site -COOHarrow_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
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY