An effective all-atom potential for proteins

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dc.creatorIrbäck, Anders
dc.creatorMitternacht, Simon
dc.creatorMohanty, Sandipan
dc.date2009-04-08
dc.date.accessioned2026-07-07T13:01:44Z
dc.date.available2026-07-07T13:01:44Z
dc.descriptionWe describe and test an implicit solvent all-atom potential for simulations of protein folding and aggregation. The potential is developed through studies of structural and thermodynamic properties of 17 peptides with diverse secondary structure. Results obtained using the final form of the potential are presented for all these peptides. The same model, with unchanged parameters, is furthermore applied to a heterodimeric coiled-coil system, a mixed alpha/beta protein and a three-helix-bundle protein, with very good results. The computational efficiency of the potential makes it possible to investigate the free-energy landscape of these 49--67-residue systems with high statistical accuracy, using only modest computational resources by today's standards.
dc.identifierhttps://arxiv.org/abs/0904.1365
dc.identifierhttp://arxiv.org/abs/0904.1365
dc.identifierPMC Biophysics 2009, 2:2
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/226248
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.titleAn effective all-atom potential for proteins
dc.typetext

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