Summary: | <p>The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and
DNA. Time-resolved NMR experiments can be conducted in a reversible or an
irreversible manner. In particular, irreversible folding experiments pose large requirements for (i) signal-to-noise due to the time limitations
and (ii) synchronising of the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the
study of time-resolved NMR studies. Further, methods are reviewed ranging
from pressure and temperature jump, light induction to rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.</p>
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