Better force fields start with better data: A data set of cation dipeptide interactions.

ABSTRACT: We present a data set from a first-principles study of amino-methylated and acetylated (capped) dipeptides of the 20 proteinogenic amino acids - including alternative possible side chain protonation states and their interactions with selected divalent cations (Ca²⁺, Mg²⁺ and Ba²⁺). The data covers 21,909 stationary points on the respective potential-energy surfaces in a wide relative energy range of up to 4 eV (390 kJ/mol). Relevant properties of interest, like partial charges, were derived for the conformers. The motivation was to provide a solid data basis for force field parameterization and further applications like machine learning or benchmarking. In particular the process of creating all this data on the same first-principles footing, i.e. density-fu

SUBMITTER: Hu X 

PROVIDER: S-EPMC9205945 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature