Narula S S, Dhingra M M
Chemical Physics Group, Tata Institute of Fundamental Research, Bombay.
J Biomol Struct Dyn. 1984 Aug;2(1):175-89. doi: 10.1080/07391102.1984.10507556.
The intramolecular conformation of puromycin, a broad spectrum antibiotic, in solution has been investigated by proton magnetic resonance (PMR) spectroscopy. A comparison of the proton chemical shift and proton-proton coupling constant data of puromycin with puromycin aminonucleoside suggests that puromycin in solution exists as an equilibrium blend of extended and folded conformers. These folded conformers are the result of flexibility around the C alpha -C beta bond of the aminoacyl segment of puromycin. One of the folded conformers predicted by PMR is in excellent agreement with the x-ray data.
通过质子磁共振（PMR）光谱法研究了广谱抗生素嘌呤霉素在溶液中的分子内构象。嘌呤霉素与嘌呤霉素氨基核苷的质子化学位移和质子 - 质子耦合常数数据比较表明，溶液中的嘌呤霉素以伸展构象和折叠构象的平衡混合物形式存在。这些折叠构象是嘌呤霉素氨酰基片段的Cα - Cβ键周围灵活性的结果。PMR预测的一种折叠构象与X射线数据非常吻合。
