Nuclear Magnetic Resonance Spectroscopy of the Circadian Clock of Cyanobacteria

• Published in: Integrative and comparative biology Vol. 53; no. 1; pp. 93 - 102
• Main Authors: Chang, Yong-Gang, Tseng, Roger, Kuo, Nai-Wei, LiWang, Andy
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.07.2013; Oxford Publishing Limited (England)
• Subjects: Bacteria; Circadian Clocks - physiology; Circadian Rhythm Signaling Peptides and Proteins - metabolism; Cyanobacteria - metabolism; Cyanobacteria - physiology; Keeping Time During Animal Evolution: Conservation and Innovation of the Circadian Clock; Magnetic fields; Magnetic Resonance Spectroscopy - methods; NMR; Nuclear magnetic resonance; Proteins
• ISSN: 1540-7063; 1557-7023
• DOI: 10.1093/icb/ict054

The most well-understood circadian clock at the level of molecular mechanisms is that of cyanobacteria. This overview is on how solution-state nuclear magnetic resonance (NMR) spectroscopy has contributed to this understanding. By exciting atomic spin-½ nuclei in a strong magnetic field, NMR obtains information on their chemical environments, inter-nuclear distances, orientations, and motions. NMR protein samples are typically aqueous, often at near-physiological pH, ionic strength, and temperature. The level of information obtainable by NMR depends on the quality of the NMR sample, by which we mean the solubility and stability of proteins. Here, we use examples from our laboratory to illustrate the advantages and limitations of the technique.