Cavalli, Andrea Camilloni, Carlo Vendruscolo, Michele 2013-03-07 In order to characterise the dynamics of proteins, a well-established method is to incorporate experimental parameters as replica-averaged structural restraints into molecular dynamics simulations. Here, we justify this approach in the case of interproton distance information provided by nuclear Overhauser effects by showing that it generates ensembles of conformations according to the maximum entropy principle. These results indicate that the use of replica-averaged structural restraints in molecular dynamics simulations, given a force field and a set of experimental data, can provide an accurate approximation of the unknown Boltzmann distribution of a system. application/pdf https://n2t.net/ark:/12658/srd1318872 https://susi.usi.ch/global/documents/318872 https://susi.usi.ch/documents/318872/files/Cavalli_JCP_2013.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1063/1.4793625 info:eu-repo/semantics/altIdentifier/ark/12658/srd1318872 info:eu-repo/semantics/openAccess License undefined The journal of chemical physics. - 2013, vol. 138, no. 9, p. 094112 info:eu-repo/classification/udc/61 Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle http://purl.org/coar/resource_type/c_6501