Which of the following can be analyzed using NMR spectroscopy?

NMR spectroscopy is particularly effective for studying the structures and dynamics of biomolecules such as proteins in their native states. It provides insights into conformational changes and protein folding by allowing scientists to observe how the environment around specific atoms in the protein changes under different conditions. This technique enables the visualization of interatomic distances, angles, and motions in real time, thereby capturing the conformational dynamics of proteins.

By utilizing NMR spectroscopy, researchers can determine the three-dimensional structure of proteins and monitor changes that occur upon ligand binding or in response to environmental changes, thereby revealing important aspects of protein behavior. The other options, while related to protein study, do not directly align with the primary capabilities of NMR spectroscopy. For example, protein crystallization conditions are more commonly analyzed using X-ray crystallography rather than NMR, which requires sufficient concentrations of proteins that are often not achievable in crystallization experiments. Similarly, thermal denaturation profiles are typically assessed through techniques such as differential scanning calorimetry or UV spectroscopy. Lastly, although NMR can be used to study membrane interactions, detailed membrane composition and structural studies are often more effectively analyzed with methods specifically designed for membrane biology. Thus, option B accurately reflects the strengths of NMR spectroscopy in studying protein dynamics.