Analysis of Backbone Dynamics of Interleukin-1β
The 15N T1, T2 and NOE data for interleukin-1β has been studied using inverse detected heteronuclear nuclear spectroscopy. It is shown that the 15N relaxation data for a number of residues cannot be accounted for by the simple two parameter model free approach of Lipari and Szabo, and require the introduction of two distinct internal motions, one with a time scale much less than 100 ps, the other with an effective correlation time in the range 0.5–4 ns, slightly less than the overall rotational correlation time (8.3 ns) of the protein.
KeywordsCorrelation Time Internal Motion Relaxation Data Spectral Density Function Rotational Correlation Time
Unable to display preview. Download preview PDF.