Small-angle X-ray scattering studies of the structure of nucleosome core histone complexes in solution |
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Authors: | Hilde Damaschun,Gregor Damaschun,Dietrich Zirwer,Rolf Misselwitz,Irina A. Zalenskaya,Vladimir I. Vorob ev |
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Affiliation: | Zentralinstitut für Molekularbiologie der Akademie der Wissenschaften der DDR, DDR-1115 Berlin-Buch, Robert-Rössle-Str.10, German Democratic Republic;Institute of Cytology, Academy of Sciences of the USSR, Leningrad 190 121, USSR |
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Abstract: | The nucleosome core histone complex in solution at 2 M NaCl and pH 7 has a radius of gyration Rs, of 3.48 nm and a maximum dimension, L, of 12 nm. Its shape is disc-like with a mean thickness of 3 nm. The radius of gyration determined by us is of the same value as the radius of gyration of the complex in intact core particles (Braddock) et al., Biopolymers 1981, 20, 327). Thus, we conclude that the basic histone tails of the protein complex project about 2 nm from its central part. |
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Keywords: | Proteins chromatin nucleosome core particles histones structure small-angle X-ray scattering |
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