Exploring the Unfolding Pathway of Maltose Binding Proteins: An Integrated Computational Approach

Carlo Guardiani, Daniele Di Marino, Anna Tramontano, Mauro Chinappi, Fabio Cecconi

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


© 2014 American Chemical Society. Recent single-molecule force spectroscopy experiments on the Maltose Binding Proteins (MBPs) identified four stable structural units, termed unfoldons, that resist mechanical stress and determine the intermediates of the unfolding pathway. In this work, we analyze the topological origin and the dynamical role of the unfoldons using an integrated approach which combines a graph-theoretical analysis of the interaction network of the MBP native-state with steered molecular dynamics simulations. The topological analysis of the native state, while revealing the structural nature of the unfoldons, provides a framework to interpret the MBP mechanical unfolding pathway. Indeed, the experimental pathway can be effectively predicted by means of molecular dynamics simulations with a simple topology-based and low-resolution model of the MBP. The results obtained from the coarse-grained approach are confirmed and further refined by all-atom molecular dynamics.
Original languageEnglish (US)
Pages (from-to)3589-3597
Number of pages9
JournalJournal of Chemical Theory and Computation
Issue number9
StatePublished - Aug 12 2014
Externally publishedYes


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