A 2D NMR study of the internal flexibility of the antifungal peptide stendomycin

التفاصيل البيبلوغرافية
العنوان: A 2D NMR study of the internal flexibility of the antifungal peptide stendomycin
المؤلفون: Simorre, J. P., Genest, D., Caille, A., Ptak, M.
المصدر: European Biophysics Journal with Biophysics Letters; July 1990, Vol. 18 Issue: 6 p309-316, 8p
مستخلص: A 2-D 1H NMR study (NOESY, COSY, HOHAHA and ROESY experiments) of the antifungal peptide stendomycin is presented. The variation of the NOESY cross peak intensities is measured as a function of temperature in order to discriminate between constant and fluctuating interproton distances. It is shown that among 71 NOESY cross peaks, only 12 correspond to well defined interproton distances and their correlation time is determined. The other cross peaks cannot be translated accurately in terms of distances owing to internal molecular motions. 1H}-13C nOe measurements confirm the internal mobility of the molecule. Finally a flexibility map of stendomycin can be established.
قاعدة البيانات: Supplemental Index
الوصف
تدمد:01757571
14321017
DOI:10.1007/BF00196921