Raman spectroscopic evidence for structural changes in poly-L-lysine induced by an approximately 50 mT static...

We have explored the mechanism of coupling of an approximately 50 mT static magnetic field with the alpha helices of poly-L-lysine. Structural changes in poly-L-lysine were determined by Raman spectroscopy. Our testable hypothesis is that static magnetic fields of this magnitude can couple with the alpha-helical segments of the polypeptide, and, as a result, the structure of the polypeptide is significantly altered. Our model further suggests that a static magnetic field can promote protein unfolding and can prevent refolding.