Articles | Volume 2, issue 1
Review article
11 May 2021
Review article |  | 11 May 2021

Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics

György Pintér, Katharina F. Hohmann, J. Tassilo Grün, Julia Wirmer-Bartoschek, Clemens Glaubitz, Boris Fürtig, and Harald Schwalbe

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Field: Liquid-state NMR | Topic: Applications – biological macromolecules
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Cited articles

Afek, A., Shi, H., Rangadurai, A., Sahay, H., Senitzki, A., Xhani, S., Fang, M., Salinas, R., Mielko, Z., Pufall, M. A., Poon, G. M. K., Haran, T. E., Schumacher, M. A., Al-Hashimi, H. M., and Gordân, R.: DNA mismatches reveal conformational penalties in protein-DNA recognition, Nature, 587, 291–296,, 2020. 
Akasaka, K.: Probing Conformational Fluctuation of Proteins by Pressure Perturbation, Chem. Rev., 106, 1814–1835,, 2006. 
Akasaka, K.: Protein Studies by High-Pressure NMR, in: Experimental Approaches of NMR Spectroscopy: Methodology and Application to Life Science and Materials Science, edited by: The Nuclear Magnetic Resonance Society of Japan, Springer, Singapore, 3–36,, 2018. 
Akasaka, K., Naito, A., Nakatani, H., and Imanari, M.: Construction and performance of a temperature-jump NMR apparatus, Rev. Sci. Instrum., 61, 66–68,, 1990. 
Akasaka, K., Naito, A., and Nakatani, H.: Temperature-jump NMR study of protein folding: Ribonuclease A at low pH, J. Biomol. NMR, 1, 65–70,, 1991. 
Short summary
The folding, refolding and misfolding of biomacromolecules including proteins, DNA and RNA is an important area of biophysical research to understand functional and disease states of a cell. NMR spectroscopy provides detailed insight, with both high time and atomic resolution. These experiments put stringent requirements on signal-to-noise for often irreversible folding reactions. The review describes methodological approaches and highlights key applications.