Minimal NMR distance information for rigidity of protein graphs

Abstract : Nuclear Magnetic Resonance (NMR) experiments provide distances between close atoms of a protein molecule and the problem is how to determine the 3D protein structure by exploiting such distances. We present a new hand-crafted order on the atoms of the protein that uses information from the chemistry of proteins and NMR experiments and allows us to formulate the problem as a combinatorial search. Additionally, this order tell us what kind of NMR distance information is crucial to understand the cardinality of the solution set of the problem and its computational complexity.
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Carlile Lavor, Leo Liberti, Bruce Donald, Bradley Worley, Benjamin Bardiaux, et al.. Minimal NMR distance information for rigidity of protein graphs. Discrete Applied Mathematics, Elsevier, 2019, 256, pp.91-104. ⟨10.1016/j.dam.2018.03.071⟩. ⟨hal-02350273⟩

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