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Kinetic factors may reshape the dependence of crystal nucleation rate on temperature in protein bulk solution

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Abstract

Here we provide an analysis of primary results obtained from a study of apoferritin crystal nucleation in compositionally invariant bulk solution at constant supersaturation ratio of the protein. The temperature dependence of the stationary crystal nucleation rate in the protein bulk solution is obtained with the help of experimentally determined probability for detection of at least one crystal per solution volume until a given time. The stationary crystal nucleation rate demonstrates unusual behavior with temperature. We emphasize that this is caused by kinetic factors that are often disregarded in the frame of the classical nucleation theory but can certainly affect the nucleation kinetics.

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References

  1. Selimovic, S., Jia, Y., Fraden, S.: Measuring the nucleation rate of lysozyme using microfluidics. Cryst. Growth Des. 9, 1806–1810 (2009)

    Article  Google Scholar 

  2. Bhamidi, V., Varanasi, S., Schall, C.A.: Measurement and modeling of protein crystal nucleation kinetics. Cryst. Growth Des. 2, 395–400 (2002)

    Article  Google Scholar 

  3. Galkin, O., Vekilov, P.G.: Direct determination of the nucleation rates of protein crystals. J. Phys. Chem. B 103, 10965–10971 (1999)

    Article  Google Scholar 

  4. Ildefonso, M., Candoni, N., Veesler, S.: Using microfluidics for fast, accurate measurement of lysozyme nucleation kinetics. Cryst. Growth Des. 11, 1527–1530 (2011)

    Article  Google Scholar 

  5. Christopher, G.K., Phipps, A.G., Gray, R.J.: Temperature-dependent solubility of selected proteins. J. Cryst. Growth 191, 820–826 (1998)

    Article  ADS  Google Scholar 

  6. Petsev, D.N., Thomas, B.R., Yau, S.-T., Tsekova, D., Nanev, C., Wilson, W.W., Vekilov, P.G.: Temperature-independent solubility and interactions between apoferritin monomers and dimers in solution. J. Cryst. Growth 232, 21–29 (2001)

    Article  ADS  Google Scholar 

  7. Dimitrov, I.L.: Crystal nucleation from solutions of proteins with temperature-independent solubility: a case study of apoferritin. CrystEngComm. 21, 1279–1287 (2019)

    Article  Google Scholar 

  8. Yau, S.-T., Petsev, D.N., Thomas, B.R., Vekilov, P.G.: Molecular-level thermodynamic and kinetic parameters for the self-assembly of apoferritin molecules into crystals. J. Mol. Biol. 303, 667–678 (2000)

    Article  Google Scholar 

  9. Kashchiev, D.: Nucleation: Basic Theory with Applications. Butterworth-Heinemann, Oxford (2000)

    Google Scholar 

  10. Kashchiev, D.: Nucleation at changing density of monomers. Cryst. Res. Technol. 20, 723–731 (1985)

    Article  Google Scholar 

  11. Jiang, S., ter Horst, J.H.: Crystal nucleation rates from probability distributions of induction times. Cryst. Growth Des. 11, 256–261 (2011)

    Article  Google Scholar 

  12. Kulkarni, S.A., Kadam, S.S., Meekes, H., Stankiewicz, A.I., ter Horst, J.H.: Crystal nucleation kinetics from induction times and metastable zone widths. Cryst. Growth Des. 13, 2435–2440 (2013)

    Article  Google Scholar 

  13. Dimitrov, I.L., Hodzhaoglu, F.V., Koleva, D.P.: Probabilistic approach to lysozyme crystal nucleation kinetics. J. Biol. Phys. 41, 327–338 (2015)

    Article  Google Scholar 

  14. Papon, P., Leblond, J., Meijer, P.H.E.: The Physics of Phase Transitions: Concepts and Applications. Springer, Dordrecht (2006)

    Book  Google Scholar 

  15. Erdemir, D., Lee, A.Y., Myerson, A.S.: Nucleation of crystals from solution: classical and two-step models. Acc. Chem. Res. 42, 621–629 (2009)

    Article  Google Scholar 

  16. Kashchiev, D., van Rosmalen, G.M.: Review: nucleation in solutions revisited. Cryst. Res. Technol. 38, 555–574 (2003)

    Article  Google Scholar 

  17. Van Driessche, A.E.S., Van Gerven, N., Bomans, P.H.H., Joosten, R.R.M., Friedrich, H., Gil-Carton, D., Sommerdijk, N.A.J.M., Sleutel, M.: Molecular nucleation mechanisms and control strategies for crystal polymorph selection. Nature 556, 89–94 (2018)

    Article  ADS  Google Scholar 

  18. Stefanini, S., Cavallo, S., Wang, C.-Q., Tataseo, P., Vecchini, P., Giartosio, A., Chiancone, E.: Thermal stability of horse spleen apoferritin and human recombinant H apoferritin. Arch. Biochem. Biophys. 325, 58–64 (1996)

    Article  Google Scholar 

  19. Pound, G.M., La Mer, V.K.: Kinetics of crystalline nucleus formation in supercooled liquid tin. J. Am. Chem. Soc. 74, 2323–2332 (1952)

    Article  Google Scholar 

  20. Kashchiev, D., Clausse, D., J.-Dalmazzone, C.: Crystallization and critical supercooling of disperse liquids. J. Colloid Interface Sci. 165, 148–153 (1994)

    Article  ADS  Google Scholar 

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Acknowledgments

The author is indebted to Prof. Dimo Kashchiev for fruitful discussions and useful suggestions in the course of the present investigation. The essentials of the experimental procedure and the data points in Fig. 2 are reproduced from Ref. [7] with permission from the Royal Society of Chemistry.

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  1. Institute of Physical Chemistry “Rostislaw Kaischew”, Bulgarian Academy of Sciences, Acad. G. Bonchev Str., bl. 11, 1113, Sofia, Bulgaria

    Ivaylo L. Dimitrov

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  1. Ivaylo L. Dimitrov
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Correspondence to Ivaylo L. Dimitrov.

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Dimitrov, I.L. Kinetic factors may reshape the dependence of crystal nucleation rate on temperature in protein bulk solution. J Biol Phys 46, 343–350 (2020). https://doi.org/10.1007/s10867-020-09558-1

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