main binding pocket inside the GLP-1 receptor and the critical residues found in GLP-1 particularly in its N-terminus. what are the amino acids found particularly in its N terminus

The figure  from Moore (2020) shows a G protein-coupled receptor in a membrane. Note that "out" means outside the cell and "in" means facing the cytoplasm. The three amino acids "DRY" in loop I2 are required  for protein targeting. What is the name of this kind  of sequence, and what is its function? What protein targeting sequence is no longer included in this diagram? Why? The sequence "QXXNK" (where X is any amino acid) found in loop I3 has been identified based on its enzymatic activity. What is this activity? What particular domain would you expect to find in either Loop E1, E2, or E3?  The gene that codes for this protein is a member of  a family of genes that has arisen over evolutionary time. If you compared several of the genes in this family, would you expect their sequences to be most homologous (similar) in the region you describe in #3 above or #4 above? Why?

During elongation eEF1α complexed to GTP escorts the aminoacyl tRNA to the ribosome. True False

If you were to remove the ER retrieval signal fromprotein disulfide isomerase (PDI), which is normally a sol-uble resident of the ER lumen, where would you expect themodified PDI to be located?

Effects of BPA on phosphorylation of MAPKfamily in RAW264.7 cells conclusion

Same question but two different sections

Expression of the muscle specific protein dystrophin is important in the functional formation of muscle tissue by     integrating the internal cytoskeleton through a transmembrane complex with the extracellular matrix.     aiding transcription factors in entry into the muscle cells nucleus     degrading non-muscle cell proteins.     none of these

From experiments in which cells expressing normal myosin II heavy chain were altered to either lack (mhckA-) or overexpress (MHCKA ++) a myosin heavy chain kinase (MHCKA). For answering this question recall the earlier the variants on the myosin II heavy chain, in which three key threonines, normally subject to reversible phosphorylation, were altered in various ways: 3X Ser = Serines in place of Threonines 3X Ala = Alanines in place of Threonines 3X Asp = Aspartate in place of Threonines MHCKA is present at normal levels. Which of the two mutants (mhcp- or MHCP++) would be most likely to have a defect in cytokinesis?

The 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.

Sars-CoV-2 spike protein: VGIYLQKTSDHRPEFALAMN What is its isoelectric point of this peptide?