NMR evidence for slow collective motions in cyanometmyoglobin.

摘要: Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations these measurements from predictions based on available crystallographic and solution structures are largely systematic well correlated within given helix this highly α-helical protein. These observations can be explained by invoking collective motion small displacements representative helices their reported average positions solid state. Thus, appear capable providing important insights into slower, motions, which likely function, difficult study using established experimental techniques.