Hydrophobic Patch Spacing Produces Nonmonotonic Compaction in Intrinsically Disordered Proteins
Henry Silvernail, Wangfei Yang, Wenwei Zheng · 2026
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Description
Henry Silvernail and co-authors show that spacing greasy patches along a floppy protein changes its size in a surprising, non-monotonic way. Their 2026 study uses computer simulations of variants of a disordered protein segment, keeping the recipe of building blocks fixed while moving the water-shunning patches apart. Average formulas based on overall greasiness cannot see arrangement effects like these.
At middle spacing the chain packed tightest; spreading patches further loosened it again. Simplified peptides revealed three possible spacing responses, not one. Which response appears depends on how strongly the patches attract and how far their reach extends. The team decomposes the shapes into patch-touching and patch-avoiding families whose tug of war sets the size. In a repulsion-driven corner, spacing even compacts chains by easing crowding. The framework unifies these cases for designers of disordered proteins.
Catalog record
| CREATOR | Henry Silvernail, Wangfei Yang, Wenwei Zheng |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 2 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |