What are some of the interactions made between ATP and the kinase? Describe bonds that the protein makes with each of the following: the phosphate groups the sugar the adenine base
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What are some of the interactions made between ATP and the kinase? Describe bonds that the protein makes with each of the following:
- the phosphate groups
- the sugar
- the adenine base
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- What are some of the interactions made between ATP and the kinase? Can you please describe bonds that the protein makes with (a) the phosphate groups, (b) the sugar, and (c) the adenine base? Please don't just copy answers from google.. I already read most of em.. :(Regarding the sodium potassium pump, I am confused which enzymes are involved in the addition of the phosphate group onto the protein to change the conformation. Is it only kinases or kinases AND ATPases? I was under the impression that kinases add organic phosphates onto molecules, while ATPases cleave ATP into ADP and a phosphate group. Would ATPase need to split the ATP molecule before the kinase can transfer the phosphate group onto the sodium potassium pump?Which of the following residues cannot be phosphorylated by a protein kinase? Ser His Thr Tyr Glu
- The predominant forms of actin inside a cell are ATP–G-actin and ADP–F-actin. Explain how the interconversion of the nucleotide state is coupled to the assembly and disassembly of actin subunits.Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?Which way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceeds
- Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R1 R2 specific interaction? name of specific interaction O yes serine tyrosine O no О yes valine threonine O no O yes threonine glutamine O no О yes cysteine cysteine noWhat is the smallest number of molecules of ATP and GTP consumed in the synthesis of a protein with 200 residues after mRNA synthesis, starting from amino acids? Assume that the hydrolysis of PP; is equivalent to the hydrolysis of ATP for this calculation. number of ATP molecules: number of GTP molecules: 400 800 IncorrectWrite a mechanism (in detail) for phosphorylation of a serine residue by ATP catalyzed by protein kinase. What groups might you expect to find in the enzyme’s active site?
- Polypeptide folding is often mediated by other proteins called chaperones. Describe how a mutant chaperone protein might be responsible for a genetic disorder involving an enzyme.A certain protein is used to activate myosin. If the protein is treated with B-mercaptoethanol, it will not activate myosin. What can you say about the structure of this protein? O The peptide is denatured by B-mercaptoethanol O The peptide does not have a thermodynamically stable configuration O The peptide contains more than one distinct chain O The peptide contains disulfide bonds required for activityIn the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe- Ser-Gin-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys The hydrophobic residues in this sequence are presented in boldface type. Use helix wheel to demonstrate this peptide is an amphipathic helix.