WHAT IF? What would happen if a mutation in the myoD gene resulted in the production of an alteredMyoD protein that could not activate the myoD gene?
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WHAT IF? What would happen if a mutation in the myoD gene resulted in the production of an altered
MyoD protein that could not activate the myoD gene?
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- WHAT IF? A certain mutation in E. coli changes the lacoperator so that the active repressor cannot bind. Howwould this affect the cell’s production of β-galactosidase?Need help:. Why is wobble proposed to hasten TL elongation?WHAT IF? The researchers needed further evidence, so they injectedbicoid mRNA into the anterior end of an egg from a female with a mutationdisabling the bicoid gene. Given that the hypothesis was supported, whatmust their results have been?
- Descrive in 2-3 sentences an in vitro experiment that differentiates between the Arp2/3 complex’ ability to associate with both the side of the ‘mother’ actin filament and with the barbed end of the ‘mother’ actin filament. Your experiment should take advantage of capping protein (binds and blocks barbed ends), and direct visualization of actin filaments.3. Please select all true answers. Myosin I is simple and often associated with the plasma membrane, myosin V is typically associated with organelle transport, and myosin II forms bundles that cause large-scale actin-myosin contractions, like those found in muscle cells. Myosins have a conserved structure that includes a head, neck and tail region. The human genome contains about 40 different myosin genes that are all orthologs of each other. Myosin proteins form a large family with many homologs The myosin head domain has an actin-binding site and a nucleotide-binding site. 4. Please select all true answers. The sliding filament assay allows the measurement of myosin activity by covalently linking fluorescent molecules directly to myosin. The myosin power stroke occurs as ATP is hydrolyzed. After a contraction, myosin needs to bind ATP to be released from actin. Shorter myosin necks allow faster movement because of a shorter power stroke.Briefly discuss the features of an ideal nanocomposite scaffold for bone tissue engineering applications. What is the composition of nanocomposite scaffolds? Describe the advantages of nanocomposite scaffolds. What is the fundamental reason of selecting nanocomposite scaffold for bone tissue engineering applications?
- Skeletal muscle myosin heavy chain is a mechanoenzyme that requires ATP for its function. Other enzymes, such as phosphofructokinase-2, also rely on ATP. How are PFK-2 and myosin Il different in their use of ATP? • View Available Hint(s) Both enzymes use ATP in the exact same way. PFK-2 functions as a kinase, whereas myosin functions as a phosphatase. PFK-2 catalyzes ATP hydrolysis, whereas myosin does not. Myosin catalyzes ATP hydrolysis, whereas PFK-2 does not. PFK-2 binds to ATP or ADP + Pj, whereas myosin undergoes covalent modification via phosphorylation. SubmitMATCHING Label the diagram below using the drop down menu provided. E Choose.. E. Choose.. Choose... D Choose... Choose... choose.Q6. The bacterium Rhizobium radiobacter is well known to biologists because it has the rather astonishing ability to cause natural genetic engineering. That is, several genes are moved from the bacterial cells directly into the nucleus of cells of many higher plant species. Expression of these transferred genes in the infected plants stimulates cell division, creating a mass of undifferentiated tissue. Which of the following signals on these transferred genes could be recognized in the plant host cell but not in the original Rhizobium cell? “TATA” box transcription terminator hairpin loop intron splice signals SD box A. 1, 2 and 3 B. 1 and 3 C. 2 and 4 D. 4 only E. All of 1, 2, 3 and 4
- 1. Which myosin type II property is most different from kinesin-1? A) myosin has two heads that can bind to cytoskeletal filamentsB) myosin is recruited into thick bipolar assembliesC) myosin hydrolyzes ATPD) myosin is an allosteric motor 2. If you were examining a newly available genome and your task was to identify the encoded family of kinesin motor proteins, what domain would be the most useful starting place for your analysis? A) Light chain #1 binding sitesB) Neck regionC) Cargo domainD) Motor domainE) Light chain #2 binding sites please explainBriefly describe an in vitro experiment that differentiate between the Arp2/3 complex’ ability to associate with both the side of the ‘mother’ actin filament and with the barbed end of the ‘mother’ actin filament. Your experiment should take advantage of capping protein (binds and blocks barbed ends), and direct visualization of actin filaments. Draw diagrams of actin filaments (simple lines are okay) that indicate the possible outcomes of your experiment. describe your interpretation of the possible outcomes for the mechanism of Arp2/3 complex-mediated branch formationWHAT IF? Imagine a protein that functions in the ERbut requires modification in the Golgi apparatus beforeit can achieve that function. Describe the protein’s paththrough the cell, starting with the mRNA molecule thatspecifies the protein.