Analysis of the entire sequence of a single photon experiment on a flavin protein.
The large amount of statistical data collected by single biomolecule experiments often demonstrates complex and non-Markovian relaxation over many time scales. Analyzing and interpreting these data is a major challenge because of the inherently statistical noise and the lack of definite theoretical descriptions or computer simulations on biologically relevant time scales. This paper reports one of the first complete sequence analyses of a single photon experiment on the flavin protein to determine an underlying physical picture for protein motions on the millisecond to second regimes. The robustness of Bayesian information analysis combined with the nonparametric maximum entropy method (MEM) incorporates all available information of the single-molecule data sequence and maximizes our ability to test the legitimacy of possible models. Our analysis of the experimental data is consistent with the stochastic Gaussian diffusion model where the slow protein motions are modeled as a collection of over-damped diffusive normal modes and reveals non-universal and distinct dynamic features that are specific for protein functions.
Witkoskie
James B
JB
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Cao
Jianshu
J
D004058:Diffusion; D005415:Flavins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D015394:Molecular Structure; D017785:Photons; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013816:Thermodynamics
D005415:Flavins; D011506:Proteins