Estimating friction coefficients of mixed globular/chain molecules, such as protein/DNA complexes.
Existing methods for predicting translational friction properties of complex molecules start by explicitly building up their three-dimensional shape with spherical subunits. This treatment has been used especially for two types of systems: rigid assemblies and flexible chain molecules. However, many protein/DNA complexes such as chromatin consist of a small number of globular, relatively rigid, bound protein interspersed by long stretches of flexible DNA chain. I present a higher level of treatment of such macromolecules that avoids explicit subunit modeling as much as possible. An existing analytical formulation of the hydrodynamics equations is shown to be accurate when used with the present treatment. Thus the approach is fast and can be applied to hydrodynamic studies of highly degenerate multiple equilibria, such as those encountered in problems of the regulation of chromatin structure. I demonstrate the approach by predicting the effect of a hypothetical unwinding process in dinucleosomes and by simulating the distribution of sedimentation coefficients for cooperative and random models for a chromatin saturation process.
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331, USA.
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Robert
D002843:Chromatin / Q000737:chemistry / Q000648:ultrastructure; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D008433:Mathematics; D008961:Models, Structural; D008962:Models, Theoretical; D009690:Nucleic Acid Conformation; D055585:Physical Phenomena; D010825:Physics; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D002843:Chromatin; D011506:Proteins; D004247:DNA