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  • CSA  (1)
  • Heteronuclear assignment  (1)
  • 1
    ISSN: 1573-5001
    Keywords: Protein ; Resonance assignment ; Automated assignment ; Heteronuclear assignment
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We present ALPS (Assignment for Labelled Protein Spectra), a flexible computer program for the automatic assignment of backbone NMR resonances of 15N/13C-labelled proteins. The program constructs pseudoresidues from peak-picking lists of a set of two-dimensional triple resonance experiments and uses either a systematic search or a simulated annealing-based optimization to perform the assignment. This method has been successfully tested on two-dimensional triple resonance spectra of Rhodobacter capsulatus ferrocytochrome c 2 (116 amino acids).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5001
    Keywords: 13C relaxation ; conformational exchange ; cross correlation ; CSA ; nucleic acids ; TROSY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A set of new NMR pulse sequences has been designed for the measurement of 13C relaxation rate constants in RNA and DNA bases: the spin-lattice relaxation rate constant R(Cz), the spin-spin relaxation rate constant R(C+), and the CSA-dipolar cross-correlated relaxation rate constant $$\Gamma _{C,CH}^{xy}$$ . The use of spin-state selective correlation techniques provides increased sensitivity and spectral resolution. Sensitivity optimised C-C filters are included in the pulse schemes for the suppression of signals originating from undesired carbon isotopomers. The experiments are applied to a 15% 13C-labelled 33-mer RNA–theophylline complex. The measured $${{R\left( {C_+} \right)} \mathord{\left/ {\vphantom {{R\left( {C_+} \right)} {\Gamma _{C,CH}^{xy} }}} \right. \kern-\nulldelimiterspace} {\Gamma _{C,CH}^{xy} }}$$ ratios indicate that 13C CSA tensors do not vary significantly for the same type of carbon (C2, C6, C8), but that they differ from one type to another. In addition, conformational exchange effects in the RNA bases are detected as a change in the relaxation decay of the narrow 13C doublet component when varying the spacing of a CPMG pulse train. This new approach allows the detection of small exchange effects with a higher precision compared to conventional techniques.
    Type of Medium: Electronic Resource
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