Peptide: difference between revisions
Diff·revision 4 → 5·16:16, 11 Jul 2024
Difference between revision 4 and revision 5 of Peptide. 2 lines changed; the page grew by 325 bytes.
| Revision 4 — 10:47, 3 Jul 2024 EndotoxinEd (talk) rm the vendor-specific packaging detail; not general enough for the article 1,981 bytes ±0 | Revision 5 — 16:16, 11 Jul 2024 CDMO_Caradoc (talk) add the excursion tolerance with the study it derives from 2,306 bytes +325 | ||
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| 15 | Peptides of fewer than about fifteen residues are usually conformationally disordered in solution, sampling many states; longer chains can adopt a persistent fold. Several of the therapeutic peptides discussed on this wiki are helical over part of their length when bound to their receptor but substantially disordered when free, which matters for how they are analysed and stored. | 15 | Peptides of fewer than about fifteen residues are usually conformationally disordered in solution, sampling many states; longer chains can adopt a persistent fold. Several of the therapeutic peptides discussed on this wiki are helical over part of their length when bound to their receptor but substantially disordered when free, which matters for how they are analysed and stored. |
| 16 | 16 | ||
| + | 17 | Side chains determine chemistry. Charged residues set the isoelectric point and therefore the pH of minimum solubility; hydrophobic residues drive [[Peptide aggregation|aggregation]]; asparagine, glutamine and methionine introduce the specific chemical liabilities discussed at [[Deamidation]] and [[Methionine oxidation]]. | |
| + | 18 | ||
| 17 | == References == | 19 | == References == |
| 18 | {{reflist}} | 20 | {{reflist}} |