title: Raman spectroscopic evidence for structural changes in poly-L-lysine induced by an approximately 50 mT static magnetic field.
abstract: 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.
authors: Department of Community Health, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
authors: S P
authors: SP
authors: Verma
authors: R B
authors: RB
authors: Goldner
mesh_terms: D008280:Magnetics; D011107:Polylysine / Q000737:chemistry / Q000528:radiation effects*; D017433:Protein Structure, Secondary / Q000528:radiation effects; D013059:Spectrum Analysis, Raman
chemical_list: D011107:Polylysine