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Explain what the likely protein sorting process would be for areceptor protein that functions to detect extracellular ligands.Include any necessary components of th...

Question

Explain what the likely protein sorting process would be for areceptor protein that functions to detect extracellular ligands.Include any necessary components of the precursor protein, and therole of proteins involved in the sorting.

Explain what the likely protein sorting process would be for a receptor protein that functions to detect extracellular ligands. Include any necessary components of the precursor protein, and the role of proteins involved in the sorting.



Answers

Sorting signals that cause retrograde transport of a protein in the secretory pathway are sometimes known as retrieval sequences. List the two known examples of retrieval sequences for soluble and membrane proteins of the ER. How does the presence of a retrieval sequence on a soluble ER protein result in its retrieval from the cis -Golgi complex? Describe how the concept of a retrieval sequence is essential to the cisternal-maturation model.

During the process of F. A. C s cells are stained with fluorescent antibodies, and this allows proteins to be located because we can see the fluorescent staining. So this type of molecule is what we require to detect cell surface proteins. So that means, in our case, to isolate the cells that contain the receptors of bacterial decorate degradation. No antibody should be directed against such a receptor. If and further, the fluorescent labeled molecule that we need must contain the receptor of interest in order to detect the bacterial degradation product.

What happens if a protein does not have a sorting signal? Well, sorting signal was tell the nuclear mechanisms where the protein should be sent so it might be sent to the enterprise. In particular, it might be sent to the Golgi apparatus for exports. If it doesn't have any signal, it goes facilities off Griffin is to be Any site is up.

Podcast. We're going to be discussing the factors protein factors more specifically involved in the process off protein synthesis. So possibly have Arnie Shay's Jean factors. We have I on i f three. So I have one in the three complex with the 30 s sub unit of our Viper Zone. And this prevents it from binding to the 50 s sub unit before the next and marina of the first tiara is in place. So next we have to. So I have to double bind to both GTP on that for a while. Matthiasson I'll t r and a uh so the first tr nay needed for the protein synthesis. So this triplex can then bind to Marina and cause the recruitment off the I f one f 3 30 s. That's fold. That's what our represent was the smallest sub unit. So this allows a 50 s subunits to associate with the 30 unit to initiate translation. So as the peptide is elongating more protein factors conf Sylhet eight this process. So we have vastly the elongation factor e f t you. This delivers in Minot a salty Arnas to the a site of the rival zone using the hydraulics ISS of GTP We don't have e f t s. So this regenerates GTP e f t you by causing the dissociation off Spend GTP from f t you. So what we generate is GTP the t u. So then we have f g. So this thing moves the, um you know, a salty Arnie's forward through three sites on the river zone. So lastly, we have the termination of the translation that's performed using protein factors, So we have a few more to consider. So we have our f one an r f to these allow the Allegra peptide to be cleaved from the final final amino a style Tianna. Then lastly, the ripe zone is disassembled using robbers own release factor.

This question asks how Dean age aeration can disrupt the function of a protein. So Dean Interational is when the three D structure of a protein is disrupted in some way. So this could happen under, like hot conditions like high heat, where the bonds that maintain the structure of the protein are broken because of that heat or other things like that. And so remember that if we're thinking about function in a protein, the structure and function of a protein are very, very closely related on. And so if you're changing the structure of the protein, you're going to change the function in most cases as well.


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