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| Titel: |
Kinetics of supersaturation decay in the crystallization of lysozyme |
| Auteur: |
KIM, Y.W. BARLOW, D.A. CARABALLO, K.G. BAIRD, J.K. |
| Verschenen in: |
Molecular physics |
| Paginering: | Jaargang 101 (2003) nr. 17 pagina's 2677-2686 |
| Jaar: |
2003-09-10 |
| Inhoud: |
The molecular architecture of proteins can be determined by analysing the X-ray diffraction patterns of their crystals. The technology of X-ray crystallography has reached the point, however, where the determination of the structure of a given crystal is controlled by the limited availability of the crystals themselves. Proteins can often be crystallized from pH buffered aqueous solutions of strong electrolytes. When dissolved protein in solution is more stable than crystalline protein, the appearance of crystals can be said to be under thermodynamic control. If, on the other hand, the crystals are more stable than the dissolved protein, and still crystals are slow to appear, the crystallization can be said to be under kinetic control. Using dilatometry, we have followed the rate of decay of the protein supersaturation in crystallizing solutions of chicken egg-white lysozyme under conditions of kinetic control. We have found that the rate of decay of the supersaturation is first order in the supersaturation and that the rate constant is independent of the initial protein concentration, but increases with increasing pH, decreasing temperature, and with increasing concentrations of sodium chloride and buffer salt. We correlate these observed trends in the rate constant with related trends in the solubility and surface charge density of the crystals. We conclude that the rate constant for supersaturation decay is inversely proportional to the protein solubility. |
| Uitgever: |
Taylor & Francis |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
Details van artikel 27 van 64 gevonden artikelen
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