Atomic structures are critical for understanding biological processes at the molecular level. NMR has become has become the most effective and reliable methodology for three-dimensional structure determination of biological macromolecules in solution. The present overview describes the basic methodology. NMR structures depend primarily on Nuclear Overhauser Effect derived distance restraints between protons close in space (<6 Å), supplemented by 3J scalar couplings that report on local dihedral angles. Large systems can be investigated using uniformly 13C/15N/2H labeled molecules and sequential assignment strategies based solely on heteronuclear through-bond correlations have become the norm. In addition, a number of recent advances, such as using Residual Dipolar Couplings for refinement and relative positioning of domains are introduced.
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Gronenborn, A.M. (2007). Some Basic Biomolecular NMR for Protein Structure Determination. In: Pifat-Mrzljak, G. (eds) Supramolecular Structure and Function 9. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6466-1_3
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