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

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 obt...

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Veröffentlicht in:Journal of biological physics 2020-12, Vol.46 (4), p.343-350
1. Verfasser: Dimitrov, Ivaylo L.
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0092-0606
1573-0689
1573-0689
DOI:10.1007/s10867-020-09558-1