Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 21, Problem 7P
Interpretation Introduction
To predict:
The result of Y161F mutation in amino acid sequence of D1 subunit of PSII.
Introduction:
Photosystem II or PSII is a specialized protein complex. Here, light energy is used to force the electron transfer from water to plastoquinone. As a result of this, oxygen is produced and reduced plastoquinone is released to photosynthetic membrane.
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Chapter 21 Solutions
Biochemistry
Ch. 21 - P700* Has the Most Negative Standard Reduction...Ch. 21 - Prob. 2PCh. 21 - Prob. 3PCh. 21 - Prob. 4PCh. 21 - The Relative Efficiency of ATP Synthesis in...Ch. 21 - pH and in the Chloroplast Proton-Motive Force...Ch. 21 - Prob. 7PCh. 21 - Prob. 8PCh. 21 - Prob. 9PCh. 21 - Prob. 10P
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- CTP synthetase catalyzes the glutamine-dependent conversion of UTP to CTP. The enzyme is allosterically inhibited by the product, CTP. Mammalian cells defective in this allosteric inhibition are found to have a complex phenotype: They require thymidine in the growth medium, they have unbalanced nucleotide pools, and they have an elevated spontaneous mutation rate. Explain the likely basis for these observations.arrow_forwardDirect mutagenesis of Ca2+ ATPase gene resulted in the replacement of two amino acid residues - Asn111 and Asn114 to Ala. These substitutions led to the reduction in Ca2+ transport activity by 10% and 50%, respectively. On the other hand, directed mutagenesis that resulted in the alteration of four Glu residues in the lumenal loop of this transport protein to Ala, did not affect the Ca2+ transport. Provide the possible explanation for the observed differences in the Ca2+ transport activity between the protein with Asn->Ala substitution and the protein with Glu->Ala substitution.arrow_forwardThe codon change (Gly-12 to Val-12) in human rasH that convertsit to oncogenic rasH has been associated with many types ofcancers. For this reason, researchers would like to develop drugs toinhibit oncogenic rasH. Based on your understanding of the Rasprotein, what types of drugs might you develop? In other words,what would be the structure of the drugs, and how would theyinhibit Ras protein? How would you test the efficacy of the drugs?What might be some side effects?arrow_forward
- GTP-y-s serves as an analog of GTP that cannot be hydrolyzed any further. How would a Co-IP experiment differ between G- alpha & G-beta proteins in the presence of GTP-y-a and GDP?arrow_forwardHuman histone H1 protein has the protein sequence as shown as “KKASKPKKAAS- KAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAPVKASKPKKAKPVK” Please propose pathway the degradation of this protein.arrow_forwardThere was a study done (Isabel, et al.) on structural analysis of SARS-CoV-2 spike protein. The researchers hypothesized that a mutation in Asp 614 to Gly 614 will result in a loss of four inter-chain destabilizing (i.e., hydrophobic-hydrophilic) contacts. I attached an image that illustrates this (C). My question is: how does this classify as a repelling effect when Asp 614 should be hydrogen bonding with Thr 859? If Asp 614 is mutated to Gly 614, then wouldn't this hydrogen bonding no longer occur? Just not too sure what this hydrophobic-hydrophilic repelling effect is referring to exactly.arrow_forward
- Which of the proteins: the CAP or the lac repressor, does the eukaryotic nuclear receptor for the glucocorticoid dexamethasone primarily resemble?arrow_forwardMany blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?arrow_forwardWhile each G-protein subunit has a distinctly characteristic C-terminal sequence that binds certain GPCRs better than others, the GPCRs that prefer the same G-protein subunit do not share a conserved sequence motif, even in the regions that form the binding pocket for the C-terminal domain of the G-protein a subunit. Given this fact, what must be similar about the binding pockets of these GPCRs in order to achieve specificity?arrow_forward
- The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.arrow_forwardThe cDNA sequence for a secreted protein shows that it contains two Asn-X-Ser/Thr motifs but nothing is known about the glycosylation of the protein. If you consider that either or both of these sites could be glycosylated and the oligosaccharides processed to either a Man5 high mannose structure or to a sialylated complex bi-antennary structure, how many possible glycoforms of the protein would there be? Explain why it is likely that such a protein would actually have very many more glycoforms.arrow_forwardCTP synthetase catalyzes the glutamine-dependent conversion of UTP to CTP. The enzyme is allosterically inhibited by the product, CTP. Mamma- lian cells defective in this allosteric inhibition are found to have a complex phenotype: They require thymidine in the growth medium, they have unbal- anced nucleotide pools, and they have an elevated spontaneous mutation rate. Explain the likely basis for these observations.arrow_forward
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