canprot: Chemical Analysis of Proteins

Chemical analysis of proteins based on their amino acid compositions. Amino acid compositions can be read from FASTA files and used to calculate chemical metrics including carbon oxidation state and stoichiometric hydration state, as described in Dick et al. (2020) <doi:10.5194/bg-17-6145-2020>. Other properties that can be calculated include protein length, grand average of hydropathy (GRAVY), isoelectric point (pI), molecular weight (MW), standard molal volume (V0), and metabolic costs (Akashi and Gojobori, 2002 <doi:10.1073/pnas.062526999>; Wagner, 2005 <doi:10.1093/molbev/msi126>; Zhang et al., 2018 <doi:10.1038/s41467-018-06461-1>). A database of amino acid compositions of human proteins derived from UniProt is provided.

Version: 2.0.0
Depends: R (≥ 3.1.0)
Imports: stringi, multcompView
Suggests: knitr, rmarkdown, tinytest, CHNOSZ (≥ 1.3.4)
Published: 2024-03-28
DOI: 10.32614/CRAN.package.canprot
Author: Jeffrey Dick ORCID iD [aut, cre]
Maintainer: Jeffrey Dick <j3ffdick at>
License: GPL-3
NeedsCompilation: no
Materials: README NEWS
CRAN checks: canprot results


Reference manual: canprot.pdf
Vignettes: Demos for canprot
Introduction to canprot
More about metrics


Package source: canprot_2.0.0.tar.gz
Windows binaries: r-devel:, r-release:, r-oldrel:
macOS binaries: r-release (arm64): canprot_2.0.0.tgz, r-oldrel (arm64): canprot_2.0.0.tgz, r-release (x86_64): canprot_2.0.0.tgz, r-oldrel (x86_64): canprot_2.0.0.tgz
Old sources: canprot archive

Reverse dependencies:

Reverse imports: chem16S


Please use the canonical form to link to this page.