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