## Abstract The present study investigates shape properties of the enzyme dUTPase from Escherichia coli in the solution phase. In this work small angle neutron scattering (SANS) findings on dUTPase/D~2~O solutions for temperature values of __T__โ=โ8โยฐC and __T__โ=โ37โยฐC are presented. The analysis
Neutron-scattering studies of the structure of chromatin core particles in solution
โ Scribed by Gordon W. Braddock; John P. Baldwin; E. Morton Bradbury
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1981
- Tongue
- English
- Weight
- 894 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
Abstract
The structure of the nucleosome core particle in solution has been studied by neutron scattering using the fullโcontrast variation technique, which reduces the experimental spectra to three fundamental scatter functions holding information on shape and structure. Systematic calculations of the fundamental scatter functions expected from proposed coreโparticle models have been compared with the observed functions and show that the neutronโscattering criteria severely restrict the number of models which can be valid for the structure in solution. The best model for the core particle in solution has a hydrophobic histone core about which 1.7 ยฑ 0.1 turns of DNA are wrapped at a pitch between 3.0 and 3.5 nm. This core contains most of the histone and has an average thickness of 4 nm and diameter 6.4โ7.5 nm. While solution scattering is not able to specify uniquely the actual shape of the core to high resolution, all models which are possible for the shape of the core to a resolution justified by the data have been considered. It is clear that cylindrical or wedge shapes compatible with the above dimensions are valid structures. A hole probably penetrates the histone core, but the data do not allow a diameter greater than 1 nm. Available evidence suggests that about a quarter of the total histone is outside the core.
๐ SIMILAR VOLUMES
Small-angle neutron scattering (SANS) was used to study the structure of protein/sodium dodecylsulfate complexes. Two water soluble proteins, bovine serum albumin (BSA) and ovalbumin (OVA), were used. The protein concentration was kept constant at 1 wt %, and protein/detergent wt ratio varied betwee
## Abstract The structures of a range of PSS combs in aqueous solutions were characterized using SLS, DLS, SANS and SAXS. Combined SLS and SANS data indicated that the comb polyelectrolytes adopted extended cylindrical structures in dilute solutions. The degree of extension of the sideโchains was a
Small angle neutron scattering (SANS) was used to characterize the micelles of cetyltrimethylammonium bromide (CTAB) in \(\mathrm{D}_{2} \mathrm{O}\) solutions, with or without added \(n\)-octylamine. SANS data have been analyzed using various models. Micellar parameters, such as mean aggregation nu