title: Nuclear magnetic resonance spectroscopy of the circadian clock of cyanobacteria.
abstract: 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-&frac12; 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.
authors.affiliation: School of Natural Sciences, University of California at Merced, Merced, CA 95343, USA.
authors.forename: Yong-Gang
authors.initials: YG
authors.lastname: Chang
authors.forename: Roger
authors.initials: R
authors.lastname: Tseng
authors.forename: Nai-Wei
authors.initials: NW
authors.lastname: Kuo
authors.forename: Andy
authors.initials: A
authors.lastname: LiWang
mesh_terms: D057906:Circadian Clocks / Q000502:physiology*; D056925:Circadian Rhythm Signaling Peptides and Proteins / Q000378:metabolism*; D000458:Cyanobacteria / Q000378:metabolism / Q000502:physiology*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*
chemical_list: D056925:Circadian Rhythm Signaling Peptides and Proteins