SMALL ANGLE X-RAY SCATTERING STUDY OF INSULIN FIBRILS
Autor: | M. V. Romanova, I. L. Maliyov, M. S. Girych, E. A. Vus, D. I. Svergun, Al. Kikhney, C. Jeffries |
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Jazyk: | English<br />Russian<br />Ukrainian |
Rok vydání: | 2015 |
Předmět: | |
Zdroj: | East European Journal of Physics, Vol 1, Iss 4, Pp 96-99 (2015) |
Druh dokumentu: | article |
ISSN: | 2312-4334 2312-4539 |
Popis: | The small-angle X-ray scattering technique was employed to determine low-resolution 3D structure of insulin amyloid fibrils. This object is of particular interest since amyloid deposits of insulin causes insulin injection amyloidosis. Structural characterization of amyloid fibrils as a particular class of linear highly ordered protein aggregates is of utmost importance for deeper understanding of the molecular etiology of conformational diseases and development of effective therapeutic strategies. The small-angle X-ray scattering pattern analysis showed that the maximum dimension of the insulin fibril cross-section reaches 24±2.4 nm, while gyration radius of the cross-section is about 6 nm. |
Databáze: | Directory of Open Access Journals |
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