Evaluating Force Matching as a Parametrization Strategy for the CHARMM36m Force Field Using Phosphorylation
Viktoria Korn, Tobias Rindfleisch, Sandra Posch, Jarl Underhaug, Andreas Horner, Markus Miettinen, Kristyna Pluhackova · 2026
Read Evaluating Force Matching as a Parametrization Strategy for the CHARMM36m Force Field Using Phosphorylation by Viktoria Korn, Tobias Rindfleisch, Sandra Posch, Jarl Underhaug, Andreas Horner, Markus Miettinen, Kristyna Pluhackova (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13244478.txt.
Description
Computer models of proteins need exact force values for tagged parts, and one common tag has rested on old guesses. Viktoria Korn and co-authors refit those values in a 2026 study. The tag is phosphorylation, a phosphate group added to a protein to switch its behavior. Their test piece stands in for a tagged serine unit and comes in several charge states.
New values were fit to match high-grade quantum results in water. Fresh lab measures then checked the fit, among them pressure readings and magnetic scan data on short tagged chains. The refit kept peace with the wider force field used in the field. Water and ion behavior around the tag came out more true to life. Better tags mean more trustworthy protein simulations.
Catalog record
| CREATOR | Viktoria Korn, Tobias Rindfleisch, Sandra Posch, Jarl Underhaug, Andreas Horner, Markus Miettinen, Kristyna Pluhackova |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 69 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |