My Best Introduction to Protein Nuclear Magnetic Resonance Spectroscopy, or Protein NMR

And an index to some chapters I’m writing with deeper content.

NMR spectra in a figure extracted from one of the chapters I’ve already released. Figure created by the author.

Introduction to the introduction

Among the atomic-resolution techniques used to study the structures of biological macromolecules, Nuclear Magnetic Resonance (NMR) spectroscopy is unique in its ability to operate in a solution state at near-room temperature. NMR spectroscopy leverages the magnetic properties of certain atomic nuclei to investigate the structure, dynamics, and interactions of biological macromolecules at atomic resolution. The process begins by placing a sample in a strong static magnetic field, typically several Tesla in strength, which aligns the magnetic spins of active nuclei such as ¹H, ¹³C, ¹⁵N, and ³¹P — elements most relevant to biological studies. These nuclei are NMR-active because they possess a net magnetic moment that interacts with the applied magnetic field. While ¹H and ³¹P are naturally abundant and easily detectable, ¹³C and ¹⁵N are less common, often requiring isotopic enrichment of samples to obtain meaningful data, especially in protein studies.

After aligning the sample in the magnetic field, one or more radiofrequency pulses are applied to perturb the magnetization of the nuclei, using…