Jj. Young et al., SOLUTION CONFORMATION OF ENOPEPTIN-A, A DEPSIPEPTIDE ANTIBIOTIC, USING 2D-NMR AND RESTRAINED MOLECULAR-DYNAMICS STUDIES, Journal of antibiotics, 47(8), 1994, pp. 922-931
Studies on the solution conformation of the cyclic depsipeptide antibi
otic enopeptin A have been carried out using 2D NMR and molecular mode
lling techniques. The proton resonances of the antibiotic in DMSO-d(6)
have been assigned by the use of TOCSY and ROESY experiments. The int
erproton distance information obtained from the ROESY experiments have
been used as the basis for elucidating the probable structures in sol
ution. The restrained molecular dynamics technique was applied to calc
ulate the structures in solution, and six resultant structures with fe
wer distance constraint violations were obtained that satisfy the expe
rimental restraints very well. The conformation of the cyclic moiety o
f the molecule is well defined whereas the aliphatic chain segment is
disordered.