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- Describe the similarities and differences in the structures of GPCRs specific for various ligands including the extracellular , transmembrane , and intracellular domains.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). In the protein adenylate kinase, the C-terminal region is a-helical, with 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. Suggest a possible reason for the periodicity in their spacing.
- ILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALEIn 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 general function and structural features of G-protein-coupled receptors (GPCRs). Be sure to include an explanation of GTPase activating proteins (GAPs) and GDP exchange factors (GEFs) in the context of the GTPase cycle. How are different classes of heterotrimeric G-proteins defined?
- 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.The Table below shows the names of proteins whose functions are regulated through the binding of their ligands. Complete this Table by filling in the correct ligands for each of the proteins, the corresponding K, value, the affinity of this protein for its ligand and the source where the protein is found. Example Protein Avidin 1 Insulin receptor 2 Anti-HIV immunoglobulin 3 Nickel binding protein 4 Myoglobin 5 Myosin 6 Acetyl-CoA carboxylase 7 Cannabinoid receptor 1 (CB1) 8 Guanylyl cyclase Ligand Biotin Kd (M) 1 x 10-15 Affinity high Source/Organism Egg whiteAt body temperature, L-aspartate in proteins race-mizes to D-aspartate at an appreciable rate. Most pro-teins in the body have a very low level of D-aspartate, if itcan be detected at all. Elastin, however, has a fairly highlevel of D-aspartate. Moreover, the amount of D-aspartateincreases in direct proportion to the age of the person fromwhom the sample was taken. Why do you suppose thatmost proteins have little if any D-aspartate, while elastinhas levels of D-aspartate that increase steadily with age?
- Describe the importance of ubiquitin-dependent degradation of soluble proteins.In trimetric G proteins the only function of the bamma y complex is to allow reactivating of the a subunit ? True or falseSignal Molecule- Somatostatin Receptor Name- Somatostatin receptor type 2 Draw the structure of the signal molecule (for peptides just sketch key motifs the best you can; i.e. alpha helices and beta sheets) discuss (100 words) the key features of the signaling cascade produced by reception of the signal molecule. along w/ 2-3 bullet points highlighting areas critical to signal amplification as well as basic mechanisms of signal termination. Cite one article