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  • 1
    Electronic Resource
    Electronic Resource
    Occurrence of β-bends in bradykinin dissolved in DMSO-d6 (1990)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 28 (1990), S. 587-593 
    Details
    ISSN: 0749-1581
    Keywords: Nuclear magnetic resonance ; Bradykinin ; β-Bend ; Nuclear Overhauser effect ; Correlated spectroscopy ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the hormone bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) in DMSO-d6 was investigated using proton NMR spectroscopy at 500 MHz. Complete resonance assignments were made using 2D COSY and NOESY techniques. The chemical shifts, magnitudes of the 3JNH-CαH couplings, temperature coefficient data on backbone NH protons and intramolecular NOEs were used to obtain information on the conformation. The nonapeptide assumes a rigid structure in DMSO-d6. Based on the experimental results, a model is proposed using computer-aided molecular graphics.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260280706
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Loss in conformational rigidity of bradykinin on replacement of the Phe-8 by tyrosine (1991)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 29 (1991), S. 333-337 
    Details
    ISSN: 0749-1581
    Keywords: Bradykinin ; [Tyr8]-bradykinin ; 1H NMR ; Conformation ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The complete resonance assignments and the conformation of the hormone [Tyr8]-bradykinin, a nonapeptide, in DMSO-d6 have been determined using 2D 1H NMR techniques. NMR parameters such as the chemical shifts, coupling constants, temperature coefficients of the backbone NH protons and NOEs have been analysed in the light of the known conformation of the native peptide. The results indicate that the peptide loses conformational rigidity on the replacement of Phe-8 by Tyr.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260290409
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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