Abstract
NMR is capable of providing many types of information about ligands, macromolecules, and their complexes. In recent years, the generation of solution structures based on NMR observations has become widespread. While these methods hold the promise of providing nearly as precise information for molecules in solution as X-ray methods do for crystals, they differ from X-ray in that the experimental observations do not reveal the ensemble of positions of all the heavy atoms, but rather the distances between certain pairs of atoms. Consequently, one needs to find tools that enable transformation from a set of pairwise distances [distance space] to Cartesian coordinate space in order to build usable structural models. These tools rely on an existing body of knowledge that describes reasonable geometries for covalently bonded atoms in amino acids and nucleotides. Most methods currently in use have their roots in molecular modeling, where computational methods have been developed to study the conformation of molecules and the relationship of conformation to biological activity.
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Beusen, D.D., Marshall, G.R. (1989). The Generation of Three-Dimensional Structures from NMR-Derived Constraints. In: Jardetzky, O., Holbrook, R. (eds) Protein Structure and Engineering. NATO ASI Series, vol 183. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5745-2_8
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DOI: https://doi.org/10.1007/978-1-4684-5745-2_8
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