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  • Chemistry  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Solution structure of salmon calcitonin (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 233-241 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Salmon calcitonin, a 32-residue peptide with a 1-7 disulfide bridge, was synthesized by standard solid-phase techniques, and studied by CD and two-dimensional NMR experiments. The peptide was dissolved in pure trifluoroethanol (TFE) and in aqueous solutions containing various amounts of TFE. CD studies in pure TFE indicated the presence of an α-helical structure comprising 40% of the constituent amino acids. This was fully confirmed by nmr. A detailed analysis was performed with the peptide in a 9 : 1 deuterated TFE/H2O mixture. A total of 365 nuclear Overhauser enhancements (154 intraresidual, 112 sequential and 99 long range) were compiled from the nuclear Overhauser enhancement spectroscopy spectra and used in the distance geometry calculations. The core of the peptide between residues 8 and 22 assumes an α-helix like structure. The Cys 1-Cys 7 ring is well defined and in close association with the helix, while the C-terminal decapeptide folds back toward the core, forming a loose loop.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310210
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  • 2
    Electronic Resource
    Electronic Resource
    Structure Elucidation of the Gallium-Ornibactin Complex by 2D-NMR Spectroscopy (1993)
    Weinheim : Wiley-Blackwell
    Liebigs Annalen 1993 (1993), S. 43-48 
    Details
    ISSN: 0170-2041
    Keywords: Ornibactin ; Siderophore ; Iron complex ; Gallium complex ; Pseudomonas strain TVV 69 ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: From a Pseudomonas strain novel hydroxamate/carboxylate siderophores were isolated which were named ornibactins representing the modified tetrapeptide L-Orn1(Nδ-OH,Nδ-acyl)-D-threo-Asp(β-OH)-L-Ser-L-Orn4(Nδ-OH,N δ-formyl)-1,4-diaminobutane. The side-chain amino function of Orn1(Nδ-OH,Nδ-acyl) is acylated by 3-hydroxyoctanoic acid in the most lipophilic component of the microheterogeneous siderophore mixture. The structure elucidation was based on GC amino acid analysis, GC-MS and electrospray mass spectrometry of the iron complex. The 3-hydroxyoctanoic acid and the primary sequence were established on the basis of 1H and inverse detected 13C two-dimensional NMR spectra (COSY, TOCSY, NOESY, HMQC, HMBC) of the gallium-ornibactin-F complex which allowed the complete assignment of all 1H and 13C signals.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jlac.199319930108
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