title: Molecular Dynamics of Biomolecules through Direct Analysis of Dipolar Couplings.
abstract: Residual dipolar couplings (RDCs) are important probes in structural biology, but their analysis is often complicated by the determination of an alignment tensor or its associated assumptions. We here apply the maximum entropy principle to derive a tensor-free formalism which allows for direct, dynamic analysis of RDCs and holds the classic tensor formalism as a special case. Specifically, the framework enables us to robustly analyze data regardless of whether a clear separation of internal and overall dynamics is possible. Such a separation is often difficult in the core subjects of current structural biology, which include multidomain and intrinsically disordered proteins as well as nucleic acids. We demonstrate the method is tractable and self-consistent and generalizes to data sets comprised of observations from multiple different alignment conditions.
authors.affiliation: †Institute for Research in Biomedicine, Via Vincenzo Vela 6, CH-6500 Bellinzona, Switzerland.|‡Laboratory of Physical Chemistry, Eidgenössische Technische Hochschule Zürich, Vladimir-Prelog-Weg 2, 8093 Zürich, Switzerland.
authors.forename: Simon
authors.initials: S
authors.lastname: Olsson
authors.affiliation: †Institute for Research in Biomedicine, Via Vincenzo Vela 6, CH-6500 Bellinzona, Switzerland.
authors.forename: Dariusz
authors.initials: D
authors.lastname: Ekonomiuk
authors.affiliation: †Institute for Research in Biomedicine, Via Vincenzo Vela 6, CH-6500 Bellinzona, Switzerland.
authors.forename: Jacopo
authors.initials: J
authors.lastname: Sgrignani
authors.affiliation: †Institute for Research in Biomedicine, Via Vincenzo Vela 6, CH-6500 Bellinzona, Switzerland.|§Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW United Kingdom.
authors.forename: Andrea
authors.initials: A
authors.lastname: Cavalli
mesh_terms: D000818:Animals; D002645:Chickens; D019277:Entropy; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D009113:Muramidase; D019696:Peptidylprolyl Isomerase; C068254:FkpA protein, E coli