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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biomolecular NMR 1 (1991), S. 391-402 
    ISSN: 1573-5001
    Keywords: Transferred nuclear Overhauser effect ; NMR ; Internal motions ; Structure determination ; Spin diffusion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In this paper we address the influence of internal motions on the development of the transferred nuclear Overhauser effect in a ligand undergoing chemical exchange between a free and a bound state. We examine the effects of varying the effective correlation time as well as the motional order parameter for methyl group and phenyl ring rotations in the free and bound ligand conformations. The effect of decreasing the motional order for a proton pair on a methyl group or phenyl ring is to decrease the effective correlation time of the internuclear vector, and thus to decrease the cross-relaxation rate between the proton pair. This functions to dampen the effects of spin diffusion, especially in the bound ligand- where cross-relaxation rates are much faster than in the free ligand. The effect of changing the effective correlation time for methyl group motions has little effect on the build-up behaviour of the transferred nuclear Overhauser effect for small values of fraction bound, but a larger effect on how fast it decays. This effect is greater for internal motions in the free peptide than it is for internal motions in the bound peptide.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 3 (1996), S. 53-60 
    ISSN: 1573-3904
    Keywords: Gramicidin S ; Cyclic peptide ; Synthesis ; Cyclization ; NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A simple method is described for the facile synthesis of gramicidin S and six other analogs, using standard solidphase synthetic technology and a single solution-phase cyclization step. The peptides were purified to homogeneity and characterized by plasma desorption time-of-flight mass spectrometry and NMR spectroscopy. Complete 1H NMR assignments for all seven peptides (in aqueous solution) are presented. Unlike previous approaches, the presented method is simple, automatable, rapid (less than three days), high-yielding, requires no side-chain protection during cyclization, and appears to be generally applicable to the preparation of a variety of related head-to-tail cyclic peptides.
    Type of Medium: Electronic Resource
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