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| 2. |
- Butorin, S. M., et al.
(author)
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Resonant inelastic soft X-ray scattering at the 4d edge of Ce-based heavy fermion materials
- 1999
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In: Journal of Electron Spectroscopy and Related Phenomena. - 0368-2048 .- 1873-2526. ; 101-103, s. 783-786
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Journal article (peer-reviewed)abstract
- Resonant X-ray scattering measurements were performed on CeB6, CeAl, γ-Ce, and α-Ce at various incident-photon energies near the Ce 4d threshold. A pronounced inelastic scattering structure which has 4f character is observed at about 4 eV below the elastic peak. The structure shows a distinct resonant behavior as well as a dependence on the degree of 4f hybridization and can therefore be attributed to charge-transfer excitations to the 4f0 state. The intensity of the elastic peak increases when going from the systems with low Kondo temperature TK to those with high TK which is consistent with a Kondo scale behavior. By analyzing the scattering data, a controversial issue on the validity of a single-impurity Anderson model in heavy-fermion materials is addressed.
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| 3. |
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| 4. |
- Butorin, SM, et al.
(author)
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Resonant inelastic soft-X-ray scattering at the 4d edge of Ce-based heavy-fermion materials
- 1999
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In: JOURNAL OF ELECTRON SPECTROSCOPY AND RELATED PHENOMENA. - 0368-2048. ; 103, s. 783-786
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Journal article (other academic/artistic)abstract
- Resonant X-ray scattering measurements were performed on CeB6, CeAl, gamma-Ce, and alpha-Ce at various incident-photon energies near the Ce 4d threshold. A pronounced inelastic scattering structure which has 4f character is observed at about 4 eV below th
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| 7. |
- Hsu, D. S., et al.
(author)
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FLOW LINEAR DICHROISM AND ELECTRON-MICROSCOPIC ANALYSIS OF PROTEIN-DNA COMPLEXES OF A MUTANT UVRB PROTEIN THAT BINDS TO BUT CANNOT KINK DNA
- 1994
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In: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836 .- 1089-8638. ; 241:5, s. 645-650
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Journal article (peer-reviewed)abstract
- (A)BC excinuclease of Escherichia coli is the enzymatic activity resulting from sequential and partially overlapping actions of UvrA, UvrB, and UvrC protein. UvrA is a molecular matchmaker which promotes the formation of a stable UvrB-damaged DNA complex in which the DNA is kinked by about 130 degrees. The UvrB-DNA complex is then recognized by UvrC) and two incisions are made in the DNA by the joint actions of UvrC and UvrB. A mutant of UvrB (D478A) can be loaded onto the DNA but it does not interact with UvrC to cause a nick 3' to the lesion. Based on the lack of a DNase-I-hypersensitive site in the footprint of the mutant, it was proposed that the lack of incision was due to the inability of the mutant UvrB to kink the DNA. In the current study we have investigated the interaction of the mutant UvrB with DNA using two biophysical methods, flow linear dichroism and electron microscopy. Both methods reveal that the mutant UvrB is unable to bend DNA.
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| 8. |
- Kim, S. K., et al.
(author)
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Binding of RecA to anti-parallel poly(dA) · 2poly(dT) triple helix DNA
- 1995
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In: Biochimica et Biophysica Acta - Gene Structure and Expression. - : Elsevier BV. - 0167-4781. ; 1264:1, s. 129-133
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Journal article (peer-reviewed)abstract
- Binding of RecA protein to conventional anti-parallel poly(dA). 2poly(dT) tripler DNA has been studied using flow linear dichroism spectroscopy. The association requires the presence of cofactor analog adenosine 5'-O-3-thiotriphosphate (ATP gamma S) and occurs with a rate similar to that for the association of RecA to double-stranded poly(dA) poly(dT) DNA. The binding of RecA to DNA stiffens the nucleotide chain, as evidenced from high orientation already at low shear rates, and the complex with tripler DNA appears to be at least as stiff as that with the duplex DNA. Therefore, the observation of a lower magnitude of the LD spectrum at 260 nm, in the triplex-RecA compared to the duplex-RecA complex, but retained magnitude of protein LD at 280 nm, indicates a markedly impaired orientation of nucleo-bases, possibly reflecting a perturbation by RecA on the third strand making its bases deviate strongly from perpendicularity. The circular dichroism spectrum: appearing immediately after dissociation of RecA by SDS, suggests an intact tripler structure, meaning that complexation with RecA has not dissociated the third strand. In conclusion, binding of RecA to tripler DNA does not modify the main organisation of the strands, but could affect the base-base interactions between them. Tilted bases could reflect a conformational change that RecA imposes also on the biological intermediate tripler structure to relax the base-base hydrogen bonding between the DNA strands.
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| 10. |
- Morse, S, et al.
(author)
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Dissociative photoionisation of OCS from threshold to 40.8 eV
- 1999
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In: INTERNATIONAL JOURNAL OF MASS SPECTROMETRY. - : ELSEVIER SCIENCE BV. - 1387-3806. ; 184:1, s. 67-74
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Journal article (other academic/artistic)abstract
- Energy-analysed photoelectrons have been measured in coincidence with product ions from photoionisation of carbonyl sulphide at 21.21 and 40.8 eV photon energy. Yields of the different products and kinetic energy release distributions in fragment ion form
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