Sedimentation equilibrium: a valuable tool to study homologous and heterogeneous interactions of proteins or proteins and nucleic acids
We present a short overview of our experience in analyzing the affinity and stoichiometry of self-associating and heterologous interactions by using the sedimentation equilibrium technique. Data acquisition and the fitting procedure employing the computer programs that we have developed, Polymole an...
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| Veröffentlicht in: | European biophysics journal 2003-08, Vol.32 (5), p.427-431 |
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| container_end_page | 431 |
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| container_title | European biophysics journal |
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| creator | Behlke, Joachim Ristau, Otto |
| description | We present a short overview of our experience in analyzing the affinity and stoichiometry of self-associating and heterologous interactions by using the sedimentation equilibrium technique. Data acquisition and the fitting procedure employing the computer programs that we have developed, Polymole and Virial, are utilized for obtaining reliable results under ideal as well as non-ideal conditions. Such data derived from biologically important macromolecules find utility in understanding physiological events such as cell regulation. |
| doi_str_mv | 10.1007/s00249-003-0318-7 |
| format | Article |
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| ispartof | European biophysics journal, 2003-08, Vol.32 (5), p.427-431 |
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| subjects | Algorithms Binding Sites Centrifugation, Density Gradient - methods Data acquisition DNA - analysis DNA - chemistry DNA-Binding Proteins - analysis DNA-Binding Proteins - chemistry Macromolecular Substances Models, Chemical Molecular biology Nucleic acids Protein Binding Proteins Proteins - analysis Proteins - chemistry |
| title | Sedimentation equilibrium: a valuable tool to study homologous and heterogeneous interactions of proteins or proteins and nucleic acids |
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