Intramolecular conformation of puromycin in solution as studied by proton magnetic resonance.
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.
D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D015394:Molecular Structure; D011522:Protons; D011691:Puromycin; D011692:Puromycin Aminonucleoside; D012996:Solutions
D011522:Protons; D012996:Solutions; D011691:Puromycin; D011692:Puromycin Aminonucleoside