During a pulse-chase experiment with secreted proteins, the proteins are synthesized for a short "pulse" time with radioactive or fluorescent amino acids to label the proteins. During the "chase" period, unlabeled amino acids are added, so any additional proteins synthesized are not labeled. The labeled proteins can then be monitored over time. You complete a pulse-chase experiment to monitor the movement of a protein. The protein is shown in the following digram. Its signal sequence is outlined and also indicated by the blue color in the primary protein structure.

You plan to synthesize a peptide to be used as a vaccine to treat melanoma, a particularly aggressive form of skin cancer. Normally, gp100, a protein on the surface of melanocytes, activates cell growth when it is bound by its ligand. Activation of the growth pathway depends on the presence of threonine in the ligand. The effective peptide vaccine will mimic the natural ligand, but won’t cause cell growth and division. Below is the sequence of the natural ligand:   LDMKTAG   In order to ensure your newly designed peptide vaccine does not cause cell growth upon binding, you must substitute the Threonine residue at position 5. What amino acid would you replace it with, bearing in mind that the peptide should still be similar enough to bind to the gp100 protein in the surface of melanocytes. Explain your choice. Your vaccine will be administered as a topical cream, and you require your peptide to have an overall neutral charge in order to be functional. At what pH should you formulate…

Which of the following is not a method for determining the high resolution structure of a folded channel protein? Group of answer choices -high resolution electron microscopy -Xray crystallography -site directed mutagenesis -Cryo electron microscopy

Regarding equations in Protein and Ligand binding.