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- Wolf-Watz, M, et al.
(author)
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Solution properties of the free and DNA-bound Runt domain of AML1.
- 1999
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In: European Journal of Biochemistry. - 0014-2956 .- 1432-1033. ; 261:1, s. 251-60
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Journal article (peer-reviewed)abstract
- The Runt domain is responsible for specific DNA and protein-protein interactions in a family of transcription factors which includes human AML1. Structural data on the Runt domain has not yet become available, possibly due to solubility and stability problems with expressed protein fragments. Here we describe the optimization and characterization of a 140-residue fragment, containing the Runt domain of AML1, which is suitable for structural studies. The fragment of AML1 including amino acids 46-185 [AML1 Dm(46-185)] contains a double cysteine-->serine mutation which does not affect Runt domain structure or DNA-binding affinity. Purified AML1 Dm(46-185) is soluble and optimally stable in a buffer containing 200 mm MgSO4 and 20 mm sodium phosphate at pH 6.0. Nuclear magnetic resonance and circular dichroism spectroscopy indicate that the Runt domain contains beta-sheet, but little or no alpha-helical secondary structure elements. The 45 N-terminal residues of AML1 are unstructured and removal of the N-terminal enhances sequence-specific DNA binding. The NMR spectrum of AML1 Dm(46-185) displays a favorable chemical shift dispersion and resolved NOE connectivities are readily identified, suggesting that a structure determination of this Runt domain fragment is feasible. A titration of 15N-labelled AML1 Dm(46-185) with a 14-bp cognate DNA duplex results in changes in the 15N NMR heteronuclear single quantum coherence spectrum which indicate the formation of a specific complex and structural changes in the Runt domain upon DNA binding.
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- Daly, AK, et al.
(author)
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Nomenclature for human CYP2D6 alleles
- 1996
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In: Pharmacogenetics. - : Ovid Technologies (Wolters Kluwer Health). - 0960-314X. ; 6:3, s. 193-201
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Journal article (peer-reviewed)
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| 5. |
- Hoffknecht, A, et al.
(author)
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Recombination of F6+ with free electrons at very low energies
- 1999
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In: Physica Scripta. Topical Issues. ; T80B, s. 298-300
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Journal article (peer-reviewed)abstract
- Radiative and dielectronic recombination of F6+ have been studied at the heavy ion storage ring TSR in Heidelberg. For a detailed investigation of rate enhancement effects at very low electron-ion center-of-mass energies experimental parameters such as the magnetic guiding field, the electron density and the adiabatic expansion factor of the electron beam have been varied systematically. Whereas measurements at different electron densities show no influence on the enhancement and while a variation of the expansion factor evokes the predicted behaviour, we see an increase of the enhancement with increasing axial magnetic field between 20 mT and 70 mT.
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