Protein dynamics using frequency-dependent order parameters from analysis of NMR relaxation data.
A novel approach is described to analyze NMR relaxation data on proteins. This method introduces the frequency-dependent order parameter, S(2)(omega), in order to estimate contributions to the generalized order parameter S(2) from different motional frequencies occurring on the picosecond to nanosecond time scales. S(2)(omega) is defined as the sum of a specified set of weighting coefficients from the Lorentzian expansion of the spectral density function. 15N NMR relaxation data (500, 600, and 800 MHz) on protein GB1 exemplify the method. Using this approach provides information on motional restrictions over specific frequency or time scale ranges and provides a normalized comparison of motional restrictions between proteins having different overall tumbling correlation times.
Idiyatullin
Djaudat
D
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota Health Science Center, 321 Church Street, Minneapolis, MN 55455, USA.
Daragan
Vladimir A
VA
Mayo
Kevin H
KH
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D009010:Monte Carlo Method; D009038:Motion; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D011994:Recombinant Proteins