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  • 1
    Electronic Resource
    Electronic Resource
    Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies (2005)
    [s.l.] : Nature Publishing Group
    Nature biotechnology 23 (2005), S. 736-740 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Segmental isotopic labeling of proteins using protein ligation is a recently established in vitro method for incorporating isotopes into one domain or region of a protein to reduce the complexity of NMR spectra, thereby facilitating the NMR analysis of larger proteins. Here we demonstrate that ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt1097
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    NMR with 13C, 15N-doubly-labeled DNA: The shape Antennapedia homeodomain complex with a 14-mer DNA duplex (1998)
    Springer
    Journal of biomolecular NMR 12 (1998), S. 25-37 
    Details
    ISSN: 1573-5001
    Keywords: isotope labeling ; nucleic acids ; protein–DNA complex ; sequential resonance assignment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Nearly complete 1H, 13C and15 N NMR assignments have been obtained for a doubly labeled 14-base pair DNA duplex in solution both in the free state and complexed with the uniformly 15N-labeled Antennapedia homeodomain. The DNA was either fully 13C,15N-labeled or contained uniformly 13C, 15N-labeled nucleotides only at those positions which form the protein–DNA interface in the previously determined NMR solution structure of the Antennapedia homeodomain–DNA complex. The resonance assignments were obtained in three steps: (i) identification of the deoxyribose spin systems via scalar couplings using 2D and 3D HCCH-COSY and soft-relayed HCCH-COSY; (ii) sequential assignment of the nucleotides via1 H–1H NOEs observed in 3D13 C-resolved NOESY; and (iii) assignment of the imino and amino groups via 1H–1H NOEs and15 N–1H correlation spectroscopy. The assignment of the duplex in the 17 kDa protein–DNA complex was greatly facilitated by the fact that 1H signals of the protein were filtered out in 13C-resolved spectroscopy and by the excellent carbon chemical shift dispersion of the DNA duplex. Comparison of corresponding 13C chemical shifts of the free and the protein-bound DNA indicates conformational changes in the DNA upon complex formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008280117211
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  • 3
    Electronic Resource
    Electronic Resource
    Arginine side chain assignments in uniformly 15N-labeled proteins using the novel 2D HE(NE)HGHH experiment (1997)
    Springer
    Journal of biomolecular NMR 10 (1997), S. 193-197 
    Details
    ISSN: 1573-5001
    Keywords: NMR assignments of arginine ; Protein structure determination ; Protein–DNA recognition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A novel 2D NMR experiment, 2D HE(NE)HGHH, is presented for the assignment ofarginine side chain 1H and 15N resonances inuniformly 15N-labeled proteins. Correlations between1Hε, 1Hγand 1Hη are established on the basis of3J(15N,1H) heteronuclear scalarcoupling constants, and sequence-specific assignments are obtained by overlapof these fragments with 1Hγ chemical shiftsobtained by assignment procedures starting from the polypeptide backbone.Since guanidino protons exchange quite rapidly with the bulk water, the 2DHE(NE)HGHH pulse scheme has been optimized to avoid saturation and dephasingof the water magnetization during the course of the experiment. As anillustration, arginine side chain assignments are presented for two uniformly15N-labeled proteins of 7 and 23 kDa molecular weight.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018381109524
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  • 4
    Electronic Resource
    Electronic Resource
    Simulation of Energy Distribution for Scanning X-ray Probe (1997)
    Chichester [u.a.] : Wiley-Blackwell
    Surface and Interface Analysis 25 (1997), S. 202-208 
    Details
    ISSN: 0142-2421
    Keywords: diffraction ; elliptical mirror ; energy distribution ; Fermi edge ; monochromator ; optical ray tracing ; rocking curve ; scanning x-ray probe ; simulation ; XPS ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The energy distribution of a scanning x-ray probe which is equipped with an elliptical mirror monochromator has been simulated with optical ray tracing, a numerically described energy distribution of Al Kα x-ray and a rocking curve. The rocking curve was estimated by dynamic diffraction theory with structure factors for quartz. The peak energy of the diffracted x-ray beam did not change with beam size, although the shapes of energy distribution were found to change slightly. Using the simulated x-ray energy distribution and the apparatus function, the energy width of the Fermi edge was simulated, which is to be compared with that obtained experimentally by monochromatic Al Kα x-ray excitation. The widths of the silver Fermi edge spectra were measured with different x-ray beam sizes. In addition, the relation between the x-ray beam position on the anode and the diffracted x-ray energy distribution was investigated. The peak energy of the diffracted x-ray beam was found to move with the x-ray beam position. It is shown that this kind of simulation can be effectively used for estimating the energy distribution and the intensity distribution of the diffracted x-ray beam. © 1997 by John Wiley & Sons, Ltd.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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