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• W2013931680 abstract "The solution properties, including hydrodynamic quantities and the radius of gyration, of globular proteins are calculated from their detailed, atomic-level structure, using bead-modeling methodologies described in our previous article (, Biophys. J. 76:3044-3057). We review how this goal has been pursued by other authors in the past. Our procedure starts from a list of atomic coordinates, from which we build a primary hydrodynamic model by replacing nonhydrogen atoms with spherical elements of some fixed radius. The resulting particle, consisting of overlapping spheres, is in turn represented by a shell model treated as described in our previous work. We have applied this procedure to a set of 13 proteins. For each protein, the atomic element radius is adjusted, to fit all of the hydrodynamic properties, taking values close to 3 A, with deviations that fall within the error of experimental data. Some differences are found in the atomic element radius found for each protein, which can be explained in terms of protein hydration. A computational shortcut makes the procedure feasible, even in personal computers. All of the model-building and calculations are carried out with a HYDROPRO public-domain computer program." @default.
• W2013931680 created "2016-06-24" @default.
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• W2013931680 date "2000-02-01" @default.
• W2013931680 modified "2023-10-17" @default.
• W2013931680 title "Calculation of Hydrodynamic Properties of Globular Proteins from Their Atomic-Level Structure" @default.
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• W2013931680 doi "https://doi.org/10.1016/s0006-3495(00)76630-6" @default.
• W2013931680 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1300675" @default.
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