"The rapidity of this folding reaction tells us something about the mechanism of protein folding. We know that folding is rapid and spontaneous because proteins can be purified then unfolded by treating them with certain chemicals that cause them to become denatured or unfolded. These denatured proteins can then be allowed to re-fold when the chemicals are removed."
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OK today I'll talk about yet another paper from Jonathan Weissman's group at UCSF ... but I'll write it up in two parts. This post will be generally background about the ER and its ability to degrade proteins.
When many scientists think about "cellular functions", diagrams of the central dogma of…
Yes this is the surprising result interpretation of Jonathan Weissman's paper in Science. For non cell biologists, click here first, to get some background on the unfolded protein response (UPR) and ER associated degradation (ERAD). And to learn about some recent developments on ERAD, click here.…
Apparently weak and strong signal sequences are differentially targeted to the ER acording to a new paper in Cell.
(For more on how proteins are inserted into the ER click here.)
Preprolactin has a strong signal sequence and is inserted into the translocon even when the unfolded protein response…
Proteins are strung together from amino acids attached in long chains, one after the other. But for most proteins, this is just the beginning - next they must fold. "Folding" is the general term for the way that a protein strand twists, coils, winds, pleats and creases into an intricate three-…