Anteunis M J, Callens R E, Tavernier D K
Eur J Biochem. 1975 Oct 15;58(2):259-68. doi: 10.1111/j.1432-1033.1975.tb02371.x.
The 1H (at 300 MHz) and 13C nuclear magnetic resonance spectra of virginiamycins S and S4 and vernamycin Balpha have been unravelled and analyzed. Together with model building and theoretical considerations, this allows the detailed description of their solution conformations. The depside bond can rotate and gives to the backbone some conformational mobility. The orientation of the depsicarbonyl bond depends on the surrounding. Apparent discrepancies between the different methods that are applicable for the disclosure of the nature of peptide H-bonding, have found a rational explanation.
已对维吉尼亚霉素S和S4以及弗氏霉素Bα的1H（300 MHz）和13C核磁共振谱进行了解析和分析。结合模型构建和理论考量，这使得能够详细描述它们在溶液中的构象。缩酚酸肽键可以旋转，使主链具有一定的构象灵活性。缩羰基键的取向取决于周围环境。适用于揭示肽氢键性质的不同方法之间明显的差异已得到合理的解释。
