title: Accuracy of current all-atom force-fields in modeling protein disordered states.
abstract: Molecular Dynamics (MD) plays a fundamental role in characterizing protein disordered states that are emerging as crucial actors in many biological processes. Here we assess the accuracy of three current force-fields in modeling disordered peptides by combining enhanced-sampling MD simulations with NMR data. These force-fields generate significantly different conformational ensembles, and AMBER03w [ Best and Mittal J. Phys. Chem. B 2010 , 114 , 14916 - 14923 ] provides the best agreement with experiments, which is further improved by adding the ILDN corrections [ Lindorff-Larsen et al. Proteins 2010 , 78 , 1950 - 1958 ].
authors.affiliation: Department of Chemistry and Applied Biosciences, Eidgenössische Technische Hochschule Zürich , CH-8093 Zurich, Switzerland.|Facoltá di Informatica, Istituto di Scienze Computazionali, Universitá della Svizzera Italiana , 6900 Lugano, Switzerland.
authors.forename: Ferruccio
authors.initials: F
authors.lastname: Palazzesi
authors.affiliation: Theoretical Sciences Unit, Jawaharlal Nehru Centre for Advanced Scientific Research , Jakkur, Bangalore, Karnataka, 500064, India.
authors.forename: Meher K
authors.initials: MK
authors.lastname: Prakash
authors.affiliation: Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, United Kingdom.
authors.forename: Massimiliano
authors.initials: M
authors.lastname: Bonomi
authors.affiliation: Laboratoire de Biophysique Statistique, Ècole Polytechnique Fèdèrale de Lausanne (EPFL) , CH-1015 Lausanne, Switzerland.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Barducci
mesh_terms: D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins