BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 31, Problem 35P
Interpretation Introduction
Interpretation:
The significance of SRP in protein translocation should be determined.
Concept introduction:
The endomembrane system is composed of ER, Golgi bodies, lysosomes, secretory vesicles, and endosomes. These cellular components are involved in the transport of proteins to outside of the cell or the other organelles of the cell. Once the protein enters the ER, it never returns to the cytosol. It is carried away by the vesicles to other cellular compartments.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Alpha polypeptide (ADH1A).
Give a detailed description of its role in the disease. Describe the impact of the disease on society.Describe a way in which your gene can be manipulated to treat the disease. Assume you can make any changes to the protein product and describe specifically how it will affect its interaction with other molecules.
proteins. 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.
True 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.
Chapter 31 Solutions
BIOCHEMISTRY
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
- Please help me with this question. More than one answer may be correct. THe graph relating to the information is included below. The figure shows the number of cells that have clusters of IRE1 molecules after those cells are treated with various levels of thapsigargin (Tg), a chemical that can induce ER stress. IRE1 can form these clusters when ER stress is induced and this clustering can cause activation of RNAse activity in IRE1. In this experiment, normal IRE1 was used (IRE1α) that can bind to Sec61, along with a modified version of IRE1 that binds to Sec61 more weakly than normal IRE1 (wIRE1α), and another modified version that binds to Sec61 more strongly than normal IRE1 (sIRE1α). From this figure you can conclude that: Question 18 options: IRE1 binding to Sec61 promotes the formation of IRE1 clumps IRE1 binding to Sec61 prevents the formation of IRE1 clumps co-translational translocation is a key process the golgi aparatus is heavily involved in the unfolded protein response The…arrow_forwardIn SDS-PAGE. What chemical is used to ensure that all protein molecules are coated with a negative charge? IPTG. β-mercaptoethanol. X-Gal. SDS.arrow_forwardAAAGAGAAAAGAAUA to AAAGAGAAAUGAAUA. Suppose the codon sequence has a single base pair mutation If the old protein sequence was Lys-Glu-Lys-Arg-Ile, what will be the new sequence encoded by the mutant gene? (Use the 3-letter amino acid abbreviations with hyphens and no spaces in between, i.e. Ser-Asn-Tyr-Leu-Pro.) Submit Answer Retry Entire Group No more group attempts remainarrow_forward
- Please 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_forwardBroken operators. Consider a hypothetical mutation in OR2OR 2 that blocks both A repressor and Cro binding. How would this mutation affect the likelihood of bacteriophage entering the lytic phase?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
- Docking 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_forwardAn extra piece. In one type of mutation leading to a form of thalassemia, the mutation of a single base (G to A) generates a new 3' 3' splice site (blue in the illustration below) akin to the normal one (yellow) but farther upstream. Normal 3' end of intron 5' CCTATTGGTCTATTITCCACCCITAGGCTGCTG 3' 5' CCTATTAGTCTAIIIICCACCCTTAGGCTGCTG 3' What is the amino acid sequence of the extra segment of protein synthesized in a thalassemic patient having a mutation leading to aberrant splicing? The reading frame after the splice site begins with TCT.arrow_forwardBONUS QUESTION! In neurons, the proteolytic enzyme y-secretase produces the Aß amyloid peptides shown below. The AB40 peptide is thought to play a protective role in the neuron. However, the AB42 peptide appears to be toxic since it is found in the amyloid plaques that cause Alzheimer's Disease (AD). AB40 and AB42 are identical, except that AB42 contains two extra amino acid residues (shown in red) at the C-terminal end. Based on your knowledge of amino acids and proteins, which of the following factors is most likely to explain the greater plaque-forming activity of AB42 compared to AB40? Sequence of Aß40: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV Sequence of AB42: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA O The greater length of AB42 makes it more likely to aggregate and form plaques. O AB42 has a lower pl than AB40, which makes it more likely to aggregate at physiological pH. O AB42 is more hydrophobic than AB40, which makes it harder to clear from the cell and thus more likely to…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_forwardI am more confused. how about we start from begining, you post answers on here, and then we go from there? 1. Identify the open reading frame in the following DNA sequence, the protein that this gene encodes for, its function, and the source. 2. "Look carefully at the DNA sequence and identify the start site for transcription" 3. Click on the DNA sequence from the start site of transcription, select all of the sequence, and copy the sequence. Go to the National Center for Biotechnology Information (NCBI) website http://www.ncbi.nlm.nih.gov/. Click on BLAST on the right-hand side under “Popular Resources.” BLAST is a program that will allow you to find the protein sequence for the DNA sequence (gene) you submit. Next click on blastx (translated nucleotide protein). Paste the DNA sequence into the box under “Entry Query Sequence.” Scroll down and click BLAST. The search may take a few seconds; the page will keep updating until the search is completed. You do not need to enter any…arrow_forwardcan you please help me out with this ? Mutations in the IL2RG gene cause approximately 30 percent of severe combined immunodeficiency disorder (SCID) cases in humans. These mutations result in alterations to a protein component of cytokine receptors that are essential for proper development of the immune system. The IL2RG gene is composed of eight exons and contains upstream and downstream sequences that are necessary for proper transcription and translation. Below are some of the mutations observed. For each, explain its likely influence on the IL2RG gene product (assume its length to be 375 amino acids). Nonsense mutation in a coding region Insertion in Exon 1, causing frameshift Insertion in Exon 7, causing frameshift Missense mutation Deletion in Exon 2, causing frameshift Deletion in Exon 2, in frame (g) Large deletion covering Exons 2 and 3arrow_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