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Small-angle X-ray scattering study of the (Fab′)2 fragment of the human immunoglobulin Kol |
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| Authors: | I. Pilz E/ Schwarz W. Palm |
| Affiliation: | Institut für Physikalische Chemie der Universität Graz, A-8010, Graz, Heinrichstrasse 28, Austria Institut für Medizinische Biochemie der Universität Graz, A-8010, Graz, Harrachgasse 21, Austria |
| Abstract: | The conformation of the (Fab′)2 fragment of the human immunoglubulin Kol has been investigated in solution by small angle X-ray scattering. The following molecular parameters were determined: radius of gyration 4.10 ± 0.05 nm; maximum distance 14.0 ± 0.5 nm and hydrated volume 150 ± 8 nm3. A model of the fragment is presented, which fits these experimental data and shows good agreement with the distance distribution function in real space and the scattering curve in reciprocal space. We have to assume that the (Fab′)2 fragment has many different conformations in solution. The method of small-angle X-ray scattering only allows the determination of an average conformation which is very similar within the resolution of the method to the static structure determined in the crystal. |
| Keywords: | Antibodies immunoglobulin crystal structure fragment small angle scattering |
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