Timeline for Loss of entropy and solvation energy in proteins
Current License: CC BY-SA 4.0
5 events
| when toggle format | what | by | license | comment | |
|---|---|---|---|---|---|
| Nov 21, 2021 at 2:54 | comment | added | Brian Blumberg | I think that the assumption the author makes is that if we only consider ion pairs, then the opposing force is greater. In other words, the ion pair is like putting on a seatbelt the wrong way. It might work preventing very slight forces but it'll just unclip if something major occurs (which is often the case in biological systems). So, the bridged form isn't unstable, just that the ion pair does little for the stability. Hopefully, Ph.D. Karsten Theis can explain this (he's edited my post and seems to know quite a bit about biochem). | |
| Nov 21, 2021 at 1:45 | history | edited | Tyberius♦ | CC BY-SA 4.0 |
added 179 characters in body
|
| Nov 21, 2021 at 1:43 | comment | added | Tyberius♦ | @BrianBlumberg if these factors were equal in magnitude, we would expect the ratio of bridged to unbridged to be 50:50. I'm assuming "poorly conserved" would be roughly within this order of magnitude, so even something like 10:90 would mean they have roughly equal energy. If "poorly conserved" is more like 1:999, then I might be interpreting the passage wrong, but I believe it saying the energies in these cases are not too different (so no preference when comparing similar proteins), rather than the bridged being very unstable in comparison. | |
| Nov 21, 2021 at 0:46 | comment | added | Brian Blumberg | Is it though? The authors state that the salt bridge itself is not a major stabilizing force because entropy and solvation fight against it. Therefore, "ion pairs are poorly conserved among homologous proteins". In other words, the magnitudes of both opposing forces are different. My question is more of why is that the case. Although correct me if I'm wrong. | |
| Nov 21, 2021 at 0:05 | history | answered | Tyberius♦ | CC BY-SA 4.0 |