What type of regulation does the interaction of BPG with hemoglobin represent?
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What type of regulation does the interaction of BPG with hemoglobin represent?
Cooperativity
Homotropic allostery
Heterotropic allostery
Covalent post-translational modification
2, 3-Bisphosphoglycerate (2,3-BPG) is most abundant organic phosphate in the red blood cell. Molar concentration of 2, 3-Bisphosphoglycerate (2,3-BPG) is approximately equivalent to that of hemoglobin.
It regulates binding of oxygen to hemoglobin.
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- Many 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)?mTOR must be tightly regulated because it controls both transcription and translation. true or false. explain whyWhat are the differences between the MWC model and the KNF model of allosteric regulation of proteins.
- Which of the following statements is true regarding the two primary classes of chaperone protein complexes in eukaryotes? O both require ATP to function, but hsp70 interacts with protein targets while they are being translated O neither require ATP, but both interact with protein targets simultaneously O hsp60 complexes are huge, and interact with protein targets during translation Ohsp70 interacts with fully synthesized proteinsAn SH2-containing protein contains a mutation that changes its binding pocket such that tyrosine and phosphotyrosine bind with equal affinity. As a result, MEK activity: does not change with receptor dimerization and transautophosphorylation decreases due to changes in Raf activation increases with ligand binding-induced dimerization decreases due to allosteric inhibition of SH2-domain bindingThe mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.
- Diisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195. Which statement is true of DIPF's inhibitory mechanism? DIPF randomly modifies all serine residues on the protein, and if enough is added, the serine in the active site will eventually be modified. DIPF approaches serine 195 more closely than other substrates. DIPF looks like the substrate for chymotrypsin and binds in the active site as a competitive inhibitor. Serine 195 is in an environment that gives it a higher than normal reactivity with respect to DIPF.While 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?Protein activity is controlled by multiple mechanisms in the cell. Briefly describe how this type of protein control is used in the cell and if this is an example of pre- or post-translational control. Allosteric activation
- Once the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes, lysyl-tRNA synthetase needs to have the proper active site in order to perform its function, explain the process of protein folding necessary to have a proper 3-D structure, include effect of thermodynamics and different states in folding, including what happen when there are prolines that form peptide bonds with other amino acids, and any disulfide bridgesDescribe the advantages and disadvantages of the following mechanisms of regulation: Transcriptional control Translational control Post translational controlWhich of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation state