Nuclear magnetic resonance spectroscopy of the circadian clock of cyanobacteria

Integr Comp Biol. 2013 Jul;53(1):93-102. doi: 10.1093/icb/ict054. Epub 2013 May 10.

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-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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Circadian Clocks / physiology*
  • Circadian Rhythm Signaling Peptides and Proteins / metabolism*
  • Cyanobacteria / metabolism
  • Cyanobacteria / physiology*
  • Magnetic Resonance Spectroscopy / methods*

Substances

  • Circadian Rhythm Signaling Peptides and Proteins