Random matrix theory in biological nuclear magnetic resonance spectroscopy.
The statistical theory of energy levels or random matrix theory is presented in the context of the analysis of chemical shifts of nuclear magnetic resonance (NMR) spectra of large biological systems. Distribution functions for the spacing between nearest-neighbor energy levels are discussed for uncorrelated, correlated, and random superposition of correlated energy levels. Application of this approach to the NMR spectra of a vitamin, an antibiotic, and a protein demonstrates the state of correlation of an ensemble of energy levels that characterizes each system. The detection of coherent and dissipative structures in proteins becomes feasible with this statistical spectroscopic technique.
D000900:Anti-Bacterial Agents; D001704:Biopolymers; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008433:Mathematics; D011487:Protein Conformation; D011506:Proteins; D013816:Thermodynamics; D014361:Trypsin Inhibitors; D014805:Vitamin B 12
D000900:Anti-Bacterial Agents; D001704:Biopolymers; D011506:Proteins; D014361:Trypsin Inhibitors; D014805:Vitamin B 12