Lysozyme fibrillation: deep UV Raman spectroscopic characterization of protein structural transformation.
Deep ultraviolet resonance Raman spectroscopy was demonstrated to be a powerful tool for structural characterization of protein at all stages of fibril formation. The evolution of the protein secondary structure as well as the local environment of phenylalanine, a natural deep ultraviolet Raman marker, was documented for the fibrillation of lysozyme. Concentration-independent irreversible helix melting was quantitatively characterized as the first step of the fibrillation. The native lysozyme composed initially of 32% helix transforms monoexponentially to an unfolded intermediate with 6% helix with a characteristic time of 29 h. The local environment of phenylalanine residues changes concomitantly with the secondary structure transformation. The phenylalanine residues in lysozyme fibrils are accessible to solvent in contrast to those in the native protein.
Xu
Ming
M
Department of Chemistry, University at Albany, SUNY, 1400 Washington Ave., Albany, NY 12222, USA.
Ermolenkov
Vladimir V
VV
He
Wei
W
Uversky
Vladimir N
VN
Fredriksen
Laura
L
Lednev
Igor K
IK
D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D009113:Muramidase / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman; D014466:Ultraviolet Rays
D000682:Amyloid; D010649:Phenylalanine; C421864:hen egg lysozyme; D009113:Muramidase