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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomolecular NMR 5 (1995), S. 59-66 
    ISSN: 1573-5001
    Keywords: Hyperbolic secant ; Constant-time HSQC ; 13C-enriched proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary An improved version of the constant-time HSQC experiment is presented that gives uniform sensitivity over the complete 13C bandwidth in 13C−1H correlation experiments without creating artifacts in the methyl and aromatic regions of the spectra. The improvement is achieved by replacing the refocussing 13C 180° pulse in the evolution time by a combination of a full-power (22 kHz) hyperbolic secant 180° pulse that inverts and refocusses the entire 13C window, immediately followed by a selective 180° pulse on the CO region. Further improvement in signal-to-noise in the aromatic and methyl regions, although less spectacular, is obtained by replacing the other two 180° 13C pulses in the INEPT parts of the pulse sequence by full-power hyperbolic secant pulses. Results of simulations and experimental data are presented that demonstrate the excellent performance of the hyperbolic secant pulse for broadband inversion and show that refocussing of transverse magnetization occurs over the same bandwidth, albeit with a 13C signal phase that depends quadratically on offset. A further modification, in which one of the selective pulses on the CO region is omitted, is also presented. Implications for other 2D and 3D experiments performed at high fields, where uniform 13C inversion and refocussing is desirable, are discussed.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-3904
    Keywords: β-turn mimic ; B1 domain ; protein engineering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A dibenzofuran-based β-turn mimic has been incorporated in the B12-29 fragment of the B1 domain of streptococcal protein G. This amino acid sequence adopts a β-hairpin structure in the complete B1 domain (B12-56). The modified peptide was studied by CD and NMR spectroscopy and its solution behavior was compared with the conformation adopted by the same sequence in the modified B1 domain.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-3904
    Keywords: β-turn mimic ; B1 domain ; protein engineering
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A dibenzofuran-based β-turn mimic has been incorporated in the B12–29 fragment of the B1 domain of streptococcal protein G. This amino acid sequence adopts a β-hairpin structure in the complete B1 domain (B12–56). The modified peptide was studied by CD and NMR spectroscopy and its solution behavior was compared with the conformation adopted by the same sequence in the modified B1 domain.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
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