## 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__β=β8βΒ°C and __T__β=β37βΒ°C are presented. The analysis
The Solution Structure of Stilbenoid Dendrimers: A Small-Angle Scattering Study
β Scribed by Sabine Rosenfeldt; Elena Karpuk; Matthias Lehmann; Herbert Meier; Peter Lindner; Ludger Harnau; Matthias Ballauff
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 155 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1439-4235
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π 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 crossβsectional radius of gyration of the deoxyribonucleoprotein (DNP) threads was measured by smallβangle Xβray scattering in a wide range of ionic strengths (from 0.0005 to 2 __M__ NaCl). For DNP in a solution of low ionic strength, this value is 30 Γ . The increase of ionic streng