Abstract
The analysis of the intact glycopeptide antibiotic, teicoplanin A 2, by two-dimensional proton NMR is described. Delayed-correlation spectroscopy (COSY), double-quantum coherence experiments (DACE), and nuclear Overhauser spectroscopy (NOESY) are utilized to confirm the primary structure. Distance constraints derived from NOESY data integrated with computer-assisted molecular modeling and force-field energy minimization yields a proposed three-dimensional solution-state conformation. Included are NMR methods developed for improved accuracy of distance measurements from 2D NOE experiments obtained on samples dissolved in DMSO- d 6/water. The effects of different pulse sequences for water suppression on the 2D NOE spectral results are compared. Clear indication that teicoplanin exists in two unequally populated conformations which are in slow exchange is revealed by the presence of cross peaks attributable to conformational interchange in the NOESY spectra.
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