Ontology highlight
ABSTRACT:
SUBMITTER: Carter-Fenk K
PROVIDER: S-EPMC10655088 | biostudies-literature | 2023 Nov
REPOSITORIES: biostudies-literature
Carter-Fenk Kevin K Liu Meili M Pujal Leila L Loipersberger Matthias M Tsanai Maria M Vernon Robert M RM Forman-Kay Julie D JD Head-Gordon Martin M Heidar-Zadeh Farnaz F Head-Gordon Teresa T
Journal of the American Chemical Society 20231102
Accurate potential energy models of proteins must describe the many different types of noncovalent interactions that contribute to a protein's stability and structure. Pi-pi contacts are ubiquitous structural motifs in all proteins, occurring between aromatic and nonaromatic residues and play a nontrivial role in protein folding and in the formation of biomolecular condensates. Guided by a geometric criterion for isolating pi-pi contacts from classical molecular dynamics simulations of proteins, ...[more]