Which technique would be most appropriate for studying the 3D structure of a protein?

Nuclear magnetic resonance (NMR) is particularly well-suited for studying the 3D structure of proteins in solution. This technique allows researchers to gather detailed information about the spatial arrangement of atoms within a protein, capturing dynamic conformations and interactions that occur in a physiological environment. By applying magnetic fields and radiofrequency radiation, NMR provides data on the distances between nuclei, which can be translated into spatial configurations of the protein structure.

Furthermore, NMR can detect changes in protein structure and dynamics, making it a powerful tool for understanding folding, flexibility, and interactions with other molecules. This ability to study proteins in a native environment adds to the accuracy and relevance of the structural data obtained through this technique, distinguishing it from methods like circular dichroism, fluorescence spectroscopy, or ultraviolet-visible spectroscopy, which provide less detailed information about 3D structures.