Abstract
In this paper, a small-angle neutron scattering study of γII-crystallins near their isoelectric point is presented. The experiments were carried out using protein concentrations of 5.7-85.7 mg/ml at temperatures in the range 11-60°C. The experimental data were analyzed using an ellipsoidal model for intraparticle correlations and the mean spherical approximation for interparticle correlations. Our studies revealed that γII-crystallins have a thick hydration layer, which is possibly due to the special arrangement of polar and ionic groups on their surface. The temperature scan shows that, as a result of relatively strong attractive forces, clusters of two, three, or higher oligomers are present below 20°C. Our results suggest that protein clusters, with a distinctive hydration layer, form a protein-rich phase that separates from a protein-lean phase as the temperature is decreased below some threshold value.
Recommended Citation
P. Petitt et al., "A Small-Angle Neutron Scattering Study of Γ-Crystallins Near their Isoelectric Point," European Journal of Biochemistry, vol. 243, no. 1 thru 2, pp. 415 - 421, FEBS Press, Jan 1997.
The definitive version is available at https://doi.org/10.1111/j.1432-1033.1997.0415a.x
Department(s)
Chemical and Biochemical Engineering
Publication Status
Free Access
Keywords and Phrases
Crystallin; Small-angle neutron scattering
International Standard Serial Number (ISSN)
0014-2956
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 FEBS Press, All rights reserved.
Publication Date
01 Jan 1997
PubMed ID
9030767
