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>.
| Version: |
0.0.2 |
| Depends: |
R (≥ 4.1.0) |
| Imports: |
bio3d, DescTools, SOMMD, tools, dplyr, tidyr, stringr, UniprotR, Rcpp |
| LinkingTo: |
Rcpp, RcppArmadillo |
| Suggests: |
httr, future, future.apply, curl, testthat (≥ 3.0.0) |
| Published: |
2026-08-25 |
| DOI: |
10.32614/CRAN.package.MDaRes (may not be active yet) |
| Author: |
Nancy D'Arminio 
[aut],
Anna Marabotti
[aut],
Alessandro Pandini
[aut, cph,
cre] |
| Maintainer: |
Alessandro Pandini <alessandro.pandini at gmail.com> |
| License: |
GPL-3 |
| NeedsCompilation: |
yes |
| Materials: |
README, NEWS |
| CRAN checks: |
MDaRes results |
Documentation:
Downloads:
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