Timeline for Why denatured proteins can't fold back in their native form
Current License: CC BY-SA 3.0
12 events
| when toggle format | what | by | license | comment | |
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| Sep 14, 2016 at 15:47 | vote | accept | KingBoomie | ||
| Sep 11, 2016 at 17:53 | comment | added | KingBoomie | Thanyou for the information! @MattDMo | |
| Sep 10, 2016 at 17:02 | history | edited | VonBeche | CC BY-SA 3.0 |
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| Sep 10, 2016 at 16:50 | comment | added | VonBeche | @MattDMo: I skimmed the Science review a bit, and it looks really really good. Turns out it's mostly "it depends", and for small (bacterial) proteins chaperones are not required, but I'll add a bit to my answer. | |
| Sep 10, 2016 at 13:25 | comment | added | MattDMo | @VonBeche here are some references. Some may be paywalled, I apologize if that's the case and you can't get access. If you really want to read one, just let me know and I'll get a PDF for you on Monday. ncbi.nlm.nih.gov/pubmed/18432918, ncbi.nlm.nih.gov/pubmed/27365453, en.wikipedia.org/wiki/Chaperone_(protein), ncbi.nlm.nih.gov/pubmed/27134861, ncbi.nlm.nih.gov/pubmed/26973652, etc. | |
| Sep 10, 2016 at 13:17 | comment | added | VonBeche | Might explain the difference. I work with bacteria, and I see a lot of heterologous proteins being expressed just fine without their own chaperones. I'll just believe you when you say it's much more common in mammalian cells. | |
| Sep 10, 2016 at 13:12 | comment | added | MattDMo | @VonBeche I'll find you some references in a minute. Yes, many chaperones are called HSPs because that is the context in which they were discovered, but further research has shown their indispensability in the "normal" cellular context (at least in mammalian cells, which I am most familiar with). | |
| Sep 10, 2016 at 13:07 | comment | added | VonBeche | @MattDMo: I think most proteins fold just fine without chaperones. In bacteria chaperones are all called heat-shock proteins, so to me it seems they're only required under stress. Do you have any sources showing that these chaperones are folding a large proportion of all proteins all the time? | |
| Sep 10, 2016 at 13:04 | comment | added | VonBeche | There would be only one energy landscape for the protein. Denatured protein in my answer is specifically aggregated denatured protein, as I assume this is what OP is talking about. A perfectly lonely heat-denatured protein would fold just as easily as a freshly synthesized one, but usually this is not the case that's discussed when talking about denatured proteins. | |
| Sep 10, 2016 at 12:53 | comment | added | MattDMo | Any discussion about protein folding also needs to include chaperones, without which many newly-synthesized proteins would not be able to fold (or re-fold after some sort of conformational "damage"). | |
| Sep 9, 2016 at 16:51 | comment | added | David | You have not explained how the 'energy landscape' differs between the newly synthesized protein (which folds) and the denatured protein (which may or may not fold). | |
| Sep 9, 2016 at 14:18 | history | answered | VonBeche | CC BY-SA 3.0 |