What is the advantage of nuclear magnetic resonance (NMR) for studying proteins?

The advantage of using nuclear magnetic resonance (NMR) for studying proteins lies in its capacity to allow observation of proteins in solution. This characteristic is particularly beneficial because it provides insights into the protein's behavior in a physiological environment, closely resembling its natural state. Unlike crystallography, which requires proteins to be crystallized and can sometimes lead to artifacts due to the rigid structure formed in crystals, NMR captures the dynamic nature and flexibility of proteins. This ability to study proteins in a more native-like environment helps researchers understand protein structure, interactions, and dynamics more accurately.

The other options present limitations relative to NMR. For example, the technique does not require large amounts of protein, making it more accessible for studying smaller or more difficult-to-isolate proteins. NMR also supports the generation of multi-dimensional data, going beyond just a two-dimensional view, thus providing a more comprehensive understanding of protein structures. It is typically more suitable for smaller proteins rather than large complexes due to limitations in resolution and spectral complexity for larger molecular sizes.