provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)
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- In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.Describe the importance of ubiquitin-dependent degradation of soluble proteins.A peptide with the sequence AELQAKSAIAHELQAKAAIAHA is treated with ATP while in the presence of kinase An alpha helix is formed with the phosphorylated at pH 5 In the direction of the helix axis, what is the length of the helix
- 12 mM of protein A is combined with 6 mM of ligand X in water. After the protein-ligand complex binding reaches equilibrium, you measure that the free ligand concentration is 3 mM and the concentration of protein-ligand complex is 3 mM. What is the Kd for protein A? Although they would be in mM, do not include units in your answer, only the number as a whole integer.Give the normal value of CRP (C-Reactive Protein). Why is CRP significant? Is CRP specific to one disease?Insulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?
- Draw a fractional binding curve for trimeric protien that has a binding site on each subunit. Moreover, the protein has a preferred low affinity conformation.Amino acids at the interaction site ( F,I and L) and its G protein partner (P, L, Y) are very conserved.If the amino acids are swapped between the protein and GPCR is binding expected to be as tight?Describe the similarities and differences in the structures of GPCRs specific for various ligands including the extracellular , transmembrane , and intracellular domains.
- Which factor has NOT been shown to play a role in determining the specificity of protein kinases? a. protein tertiary structure b. protein quaternary structure c. primary sequence at phosphorylation site d. disulfide bonds near the phosphorylation site e. residues near the phosphorylation siteThree different ligands, Ligand Q, Ligand T, and Ligand W, bind to the same protein but with different affinity: The association constant (Ka) for the binding of Ligand Q to the protein is 0.033 nM-1. The fractional saturation (Y) of the protein is 0.20 when the concentration of Ligand T is 1.25 nM. The fractional saturation (Y) of the protein is 0.80 when the concentration of Ligand W is 72 nM. Given this information, Calculate Kd for the binding of each ligand to this protein. Which ligand binds with greatest affinity? Which ligand binds with the lowest affinity?Which of the following situations would produce a Hill plot with nH < 1.0? Explain your reasoning in each case.(a) The protein has multiple subunits, each with a single ligand-binding site. Binding of ligand to one site decreases the binding affinity of other sites for the ligand.(b) The protein is a single polypeptide with two ligand-binding sites, each having a different affinity for the ligand.(c) The protein is a single polypeptide with a single ligand-binding site. As purified, the protein preparation is heterogeneous, containing some protein molecules that are partially denatured and thus have a lower binding affinity for the ligand.