BIOLOGY
12th Edition
ISBN: 9781260169614
Author: Raven
Publisher: RENT MCG
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Chapter 18, Problem 7A
Summary Introduction
Introduction:
The comparative proteomics study involves comparison between proteomes (entire proteins that can be expressed by cells) from different tissues or cells from different sets of conditions. The main goal of this is to analyze changes in proteome in response to disease, development or environment.
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Which description applies to alternative mRNA splicing?
1. heritable changes in gene expression that occur without altering the DNA sequence
2. processing of exons in mRNA that results in a single gene coding for multiple proteins
3. mRNA modifications such as additions of a 5′‑cap and 3′ poly‑A tail and removal of introns
4. a gene cluster controlled by a single promoter that transcribes to a single mRNA strand
5. protein modifications such as addition of a functional group or structural changes such as folding
Answer 2 is correct.
Mass spectrometry is a powerful tool in proteomics. What are the four key features of a mass spectrometer? Describe briefly how MALDI and two-dimensional polyacrylamide gel electrophoresis could be used to identify a protein expressed in cancer cells but not in normal healthy cells.
PROTEIN X HAS THE POTENTIAL FOR MEDICAL APPLICATION IN HUMAN. IT IS ORIGINALLY FROM A PLANT AND HAD BEEN SUCCESSFULLY CLONED FROM ITS GENE. AFTER MANY ATTEMPTS TO CLONE IT INTO EUKARYOTIC EXPRESSION VECTORS WERE UNSUCCESSFUL, THE RESEARCHER DECIDED TO USE E.COLI EXPRESSION VECTOR.
HOW THE RECOMBINANT PROTEIN COULD BE EXPRESSED IN E.COLI EXPRESSION VECTOR.1. FACTORS AFFECTING BACTERIAL EXPRESSION SYSTEM.2. STRATEGIES TO IMPROVE THE PROTEIN EXPRESSION.3. WAYS TO ENSURE THE PROTEIN IS ACTIVELY PRODUCED.
Chapter 18 Solutions
BIOLOGY
Ch. 18.1 - Prob. 1LOCh. 18.1 - Describe the pros and cons of restriction mapping,...Ch. 18.1 - Prob. 3LOCh. 18.2 - Discriminate between dideoxy terminator sequencing...Ch. 18.2 - Prob. 2LOCh. 18.3 - Describe the findings of the Human Genome Project.Ch. 18.3 - Prob. 2LOCh. 18.3 - Prob. 3LOCh. 18.4 - Prob. 1LOCh. 18.4 - Prob. 2LO
Ch. 18.4 - Prob. 3LOCh. 18.5 - Prob. 1LOCh. 18.5 - Prob. 2LOCh. 18.5 - Prob. 3LOCh. 18.6 - Prob. 1LOCh. 18 - Prob. 1DACh. 18 - If the human genome contains approximately 3...Ch. 18 - Prob. 1IQCh. 18 - Prob. 2IQCh. 18 - Prob. 3IQCh. 18 - Prob. 4IQCh. 18 - Prob. 5IQCh. 18 - Prob. 6IQCh. 18 - A genetic map provides a. the sequence of the DNA...Ch. 18 - Prob. 2UCh. 18 - Approximately how many genes are there in the...Ch. 18 - An open reading frame (ORF) is distinguished by...Ch. 18 - What is a BLAST search? a. A mechanism for...Ch. 18 - Prob. 6UCh. 18 - Prob. 7UCh. 18 - Prob. 8UCh. 18 - Prob. 1ACh. 18 - Prob. 2ACh. 18 - Prob. 3ACh. 18 - Prob. 4ACh. 18 - What information can be obtained from a DNA...Ch. 18 - Prob. 6ACh. 18 - Prob. 7ACh. 18 - You are in the early stages of a genome-sequencing...Ch. 18 - Genomic research can be used to determine if an...
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- Wassif et al. created a mouse knockout of DHCR7 (7-dehydrocholesterol reductase) gene. A.) Which disease or medical problem did Wassif et al. want to tackle with this mouse knockout? (If you cannot remember you may describe it.) B.) How did the phenotype of their mouse model differ from those of patients who had mutations in DHCR7 gene? And how was it similar? C.) What is one reason to explain the differences between the DHCR7 mouse knockout model and human patients with the mutations in the DHCR7 gene OTHER THAN the fact that they are two different organisms with differences in their biology? D.) With your BIOL2299 expertise, assume you generate a mouse knockout model of a human disease. Imagine one real world outcome from your study which can be applied in a clinical setting to help patients with that disease. Answer in one or two sentences.arrow_forwardConsider a gene sequence whose promoter has acquired a mutation. Although this is a problem, this will not cause a missense mutation. Explain why the outcome in this scenario is NOT a missense mutation. Describe the purpose of a gene's promoter.arrow_forwardThe figure shows the position of two of these mutations a and b. The nucleotides are altered in these 2 different swo-1 mutant alleles. Use the genetic table to describe any AA changes.Name the type of mutation and describe its effect on swo-1 mRNA and protein for each of the mutations. 3. The swo-1 a mutation (insertion between C and G). 4. The swo-1 b mutation (C-to-T mutation for indicated C). 5. The swo-1 a mutation leads to worms with more body wall muscle, whereas worms with the swo-1 b mutation are not able to move. Based on these phenotypes and the findings from questions 3 and 4, describe the role thewild-type version of this protein plays in muscle function.arrow_forward
- Design a strategy to make a subtracted-complete cDNA library from liver cells. Use a flowchart method to propose how this objective can be accomplished. The sizes of mRNA range from 2 kb to 15 kb. Briefly indicate your reasons for the sequence of steps..arrow_forwardGiven: eukaryotic cells can make different proteins, using only one gene. How can a eukaryotic cell make different final proteins from the same gene? Note: some of the answers are actually correct statements, but they don't have anything to do with this question. A.Eukaryotes have 3 RNA polymerases instead of just one. B.Eukaryotes cannot perform simultaneous transcription and translation. C.Eukaryotes splice RNA and can do so in various arrangements. D.Eukaryotes lack the Shine Delgarno sequence.arrow_forwardIdentify the best match between the mutation description and term. a. Transversion: results in a change in single nucleotide from a purine to another purine or a pyrimidine to another pyrimidine b. Nonsense mutation: a change in the DNA that changes the codon code from one amino acid to another amino acid c. Missense mutation: causes a drastic change in phenotype because the change causes a premature stop in the amino acid sequence d. Indel: has the potential to cause large changes in transcription and subsequence amino acid sequence due to reading frameshiftsarrow_forward
- Could quantitative PCR, which uses a DNA-binding dye, to show how many copies of the target DNA sequence could be used to quantify the amount of mRNA in a cell? Would you expect that a metabolically active tissue such as the liver would show more cDNA copies in such a method, compared to less metabolically active tissues such as skin cells? One reason that the types and amounts of mRNAs are quantified in different tissue types is to compare which genes are activated and which are inactive. It used to be thought that any gene that was transcribed was automatically translated. The discovery of RNA-degrading systems shows that the real situation in cells is more complemented. Do you believe that a larger amount of mRNA of a given type, say for alpha hemoglobin in immature red blood cells is a reliable indicator that more alpha hemoglobin protein will be made in those cells?arrow_forwardTelomerase is an attractive cancer target since 85% - 90% of tumors express telomerase (while normal cells express little to no telomerase). One paradigm in this model is the “cancer stem cell” hypothesis. Cancer stem cells (or tumor-initiating cells with stem-cell like properties) can self-renew, as well as give rise to heterogeneous tumor cell populations (essentially, they are believed to be responsible for the formation and maintenance of the tumor). If these cells are indeed “stem-like” they also divide more slowly, and presumably express telomerase (like normal stem cells).Do you think a treatment strategy that inhibits telomerase would be effective in treating cancer? How does the cancer stem cell hypothesis complicate or compliment these strategies? Justify your answer.arrow_forwardYou are studying pancreatic cancer have matched samples of tumor and healthy pancreatic tissue. You use a microarray to determine gene expression differences between these two sample. You label the healthy tissue cDNA with red fluorescnce and the tumor cDNA with green. You apply these cDNAs to your chip. Beta-actin is a housekeeping gene required for cell structure. What color would you expect the spot for this gene to be? a. Red b. Green c. Yellow d. No color e. None of the abovearrow_forward
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