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ARIA for solution and solid-state NMR.

Abstract : In solution or solid-state, determining the three-dimensional structure of biomolecules by Nuclear -Magnetic Resonance (NMR) normally requires the collection of distance information. The interpretation of the spectra containing this distance information is a critical step in an NMR structure determination. In this chapter, we present the Ambiguous Restraints for Iterative Assignment (ARIA) program for automated cross-peak assignment and determination of macromolecular structure from solution and solid-state NMR experiments. While the program was initially designed for the assignment of nuclear Overhauser effect (NOE) resonances, it has been extended to the interpretation of magic-angle spinning (MAS) solid-state NMR data. This chapter first details the concepts and procedures carried out by the program. Then, we describe both the general strategy for structure determination with ARIA 2.3 and practical aspects of the technique. ARIA 2.3 includes all recent developments. such as an extended integration of the Collaborative Computing Project for the NMR community (CCPN), the incorporation of the log-harmonic distance restraint potential and an automated treatment of symmetric oligomers.
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Benjamin Bardiaux, Thérèse Malliavin, Michael Nilges. ARIA for solution and solid-state NMR.. Protein NMR Techniques, 831, pp.453-83, 2012, ⟨10.1007/978-1-61779-480-3_23⟩. ⟨pasteur-01459144⟩



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