How protein fold: Insights from nuclear magnetic resonance spectroscopy

Many devastating diseases are linked to an imbalance in protein folding. Efficient and correct protein folding is crucial for protein functions, including catalysis, molecular recognition, molecular transport, and cellular signaling. Additionally, if protein folding is unsuccessful or the protein cannot remain in its folded state, the accumulation of misfolded species results in many pathological conditions, including neurodegenerative diseases, cancers, diabetes, and cardiovascular diseases. Not surprisingly, despite advances in our understanding of protein folding, it remains one of the fundamental questions in biology and biomedicine. Here, I discuss current experimental approaches for the characterization of protein folding using solution Nuclear Magnetic Resonance (NMR) spectroscopy.