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A New Possibility to Recognize the Concentration Dependence of Sedimentation Coefficients

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Analytical Ultracentrifugation VIII

Part of the book series: Progress in Colloid and Polymer Science ((PROGCOLLOID,volume 131))

Abstract

The binding constants of self-associating proteins can be determined from sedimentation velocity runs using the numerical solution of the Lamm equation. This procedure requires good starting values of sedimentation and diffusion coefficients or their possible concentration dependencies. We found, based on fits of synthetic data files, a connection between the concentration dependence of sedimentation coefficients (ks) and the estimated radius position at the cell base (rb). Deviation of the estimated rb value from the expected one is indicating the occurrence of ks that can be estimated by the program LammNum as a prerequisite for the calculation of reliable binding constants.

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References

  1. Behlke J, Heidrich K, Naumann M, Müller E-C, Otto A, Reuter R, Kriegel T (1998) Biochemistry 37:11989

    Article  CAS  Google Scholar 

  2. Golbik R, Naumann M, Otto A, Müller E-C, Behlke J, Reuter RR, Hübner G, Kriegel TM (2001) Biochemistry 40:1083

    Article  CAS  Google Scholar 

  3. Frigon RP, Timasheff SN (1975) Biochemistry 14:4559

    CAS  Google Scholar 

  4. Claverie J-M, Dreux H, Cohen R (1975) Biopolymers 14:1685

    Article  CAS  Google Scholar 

  5. Schuck P (1998) Biophys J 75:1503

    CAS  Google Scholar 

  6. Schuck P (2003) Analytical Biochem 320:104

    CAS  Google Scholar 

  7. Behlke J, Ristau O (2005) LAMMNUM: A Program to Study Self-Associating Macromulecules in Sedimentation Velocity Experiments. In: Scott DJ, Harding SE (eds) Modern Analytical Ultracentrifugation: Techniques and Methods. Royal Society of Chemistry UK p 122–132

    Google Scholar 

  8. Rowe AJ (1992) The Concentration Dependence of Sedimentation. In: Harding SE, Rowe AJ, Horton JC (eds) Analytical Ultracentrifugation in Biochemistry and Polymer Science p 394–406

    Google Scholar 

  9. Adams ET Jr (1992) Sedimentation Coefficients of Self-Associating Species. In: Harding SE, Rowe AJ, Horton JC (eds) Analytical Ultracentrifugation in Biochemistry and Polymer Science p 407–427

    Google Scholar 

  10. Teller DC (1973) Characterization of Proteins by Sedimentation Equilibrium in the Analytical Ultracentrifuge. In: Hirs CHW, Timasheff SN (eds) Methods in Enzymology, Vol XXVII. Academic Press, New York, p 346

    Google Scholar 

  11. Kumosinski TF, Pessen H (1985) Structural Interpretation of Hydrodynamic Measurements of Proteins in Solution through Correlations with X-Ray Data. In: Hirs CHW, Timasheff SN (eds) Methods in Enzymology, Vol 117. Academic Press, New York, p 154

    Google Scholar 

  12. Pikuleva IA, Tesh K, Waterman MR, Kim Y (2000) Arch Biochem Biophys 373:44

    Article  CAS  Google Scholar 

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Correspondence to Joachim Behlke .

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Christine Wandrey Helmut Cölfen

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Behlke, J., Ristau, O. A New Possibility to Recognize the Concentration Dependence of Sedimentation Coefficients. In: Wandrey, C., Cölfen, H. (eds) Analytical Ultracentrifugation VIII. Progress in Colloid and Polymer Science, vol 131. Springer, Berlin, Heidelberg. https://doi.org/10.1007/2882_003

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