('13)C NMR spectra were recorded for nucleosome cores and nucleosome cores with specific segments removed in an effort to identify regions of histone mobility in the nucleosome core. / Three types of particles were generated by limited proteolysis of nucleosome cores. Brief (alpha)-chymotrypsin treatment yielded a particle in which H3 residues 1-20 had been removed. Further (alpha)-chymotrypsin treatment of this particle yielded a particle in which H3 residues 1-20, H2B residues 1-18, and H4 residues 1-22 were absent. Very brief digestion of this particle with trypsin produced a particle in which H3 residues 1-20, H2B residues 1-18, H4 residues 1-22, and H2A residues 1-11 and 119-128 were removed. Comparisons of ('13)C NMR spectra of proteolysed nucleosome core particles with ('13)C NMR data of native nucleosome cores and the compositions of different peptide regions with potential mobility showed that the random coil regions observed in the core particles were located in H3 residues 1-23 and H2A residues 1-16 and 116-128. Particles with the N-terminal tails removed still retained sedimentation and circular dichroism characteristics similar to intact core particles. / Random coil resonances were also seen in preparations of nucleosome oligomers, nucleosome oligomers depleted of H1 and H5, nucleosome oligomers in a condensed form, and in intact nuclei. These resonances appeared to be very similar to those appearing in the nucleosome core spectrum. No segmental motion was seen for H1 or H5 although side chain resonances (Lys, Ala, and Thr) were observed. Very little change was seen in the ('13)C NMR spectra for nucleosome oligomers going from an extended configuration to a more condensed form. / Source: Dissertation Abstracts International, Volume: 46-06, Section: B, page: 1791. / Thesis (Ph.D.)--The Florida State University, 1985.
| Identifer | oai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_75602 |
| Contributors | SMITH, ROBERT MOSS, II., Florida State University |
| Source Sets | Florida State University |
| Detected Language | English |
| Type | Text |
| Format | 205 p. |
| Rights | On campus use only. |
| Relation | Dissertation Abstracts International |
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