MD Analysis of Residue Properties Using Structural Alphabets R package MDaRes version 0.0.2 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>. Software 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) Alessandro Pandini <alessandro.pandini@gmail.com> Comprehensive R Archive Network (CRAN) Nancy D'Arminio [aut] (ORCID: <https://orcid.org/0000-0002-8065-2142>), Anna Marabotti [aut] (ORCID: <https://orcid.org/0000-0002-9510-5205>), Alessandro Pandini [aut, cph, cre] (ORCID: <https://orcid.org/0000-0002-4158-233X>) GPL-3 2026-08-25 application/tgz https://CRAN.R-project.org/package=MDaRes doi:10.32614/CRAN.package.MDaRes