MDaRes
MD Analysis of Residue Properties Using Structural Alphabets
Analyze molecular dynamics (MD) simulation data using structural alphabets. Protein local conformations from molecular simulations are encoded in a compressed string representation. Residue-level UniProt annotations can be directly retrieved. Comparative analysis tools are available to investigate conformational variability, coordinated motions, and differences between systems (e.g. wild-type vs mutant; bound vs unbound). Methodological details for the structural alphabet analysis can be found in Pandini et al. (2013) <doi:10.1093/bioinformatics/btt326>.
Versions across snapshots
| Version | Repository | File | Size |
|---|---|---|---|
0.0.2 |
rolling linux/jammy R-4.5 | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
rolling linux/noble R-4.5 | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
rolling source/ R- | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
latest linux/jammy R-4.5 | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
latest linux/noble R-4.5 | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
latest source/ R- | MDaRes_0.0.2.tar.gz |
7.1 MiB |
0.0.2 |
2026-04-23 source/ R- | MDaRes_0.0.2.tar.gz |
0 B |