2026-04-13T06:35:07Zhttps://recercat.cat/oai/requestoai:recercat.cat:2445/1107152025-12-04T21:11:49Zcom_2072_1057col_2072_478781col_2072_478908col_2072_478917
RECERCAT
author
Emperador, Agustí
author
Orozco López, Modesto
2017-05-09T15:10:17Z2018-02-03T23:01:16Z2017-02-032017-05-09T15:10:18Z
We present a refinement of the Coarse Grained PACSAB force field for Discrete Molecular Dynamics (DMD) simulations of proteins in aqueous conditions. As the original version, the refined method provides good representation of the structure and dynamics of folded proteins but provides much better representations of a variety of unfolded proteins, including some very large, impossible to analyze by atomistic simulation methods. The PACSAB/DMD method also reproduces accurately aggregation properties, providing good pictures of the structural ensembles of proteins showing a folded core and an intrinsically disordered region. The combination of accuracy and speed makes the method presented here a good alternative for the exploration of unstructured protein systems.
(c) American Chemical Society, 2017 info:eu-repo/semantics/openAccess
Biomolècules
Dinàmica molecular
Proteïnes
Biomolecules
Molecular dynamics
Proteins
Discrete Molecular Dynamics Approach to the Study of Disordered and Aggregating Proteins
info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion