Parametrization

Note

This is just a short summary. Details for the interested can be found in our journal article [Wacha2019].

The most peculiar feature of β-peptides is their folding. In a similar fashion as for α-peptides and proteins, the secondary structure is controlled and defined by: - intrachain hydrogen bonding between the peptide bonds - sidechain configuration - backbone torsions

The first two are not expected to be different, but the third one is the one which puts β-peptides apart from their natural analogues. Therefore, in order to make a force field developed and tested for proteins and α-peptides work on β-peptides as well, backbone torsion parameters have to be re-parametrized.

The CHARMM force field family is parametrized against ab initio electronic structure simulations of simple molecules.

#TODO

[Zhu2010]

Zhu, Koenig, Hoffmann, Yethiraj, Cui. Journal of Computational Chemistry (2010) DOI: 10.1002/jcc.21493

[Wacha2019]

Wacha, Nagy, Beke-Somfai. ChemPlusChem (2019) 84, 927-941. DOI: 10.1002/cplu.201900180