Lysozyme fibrillation: Deep UV Raman spectroscopic characterization of protein structural transformation

• Published in: Biopolymers 2005-09, Vol.79 (1), p.58-61
• Main Authors: Xu, Ming, Ermolenkov, Vladimir V., He, Wei, Uversky, Vladimir N., Fredriksen, Laura, Lednev, Igor K.
• Format: Article
• Language: English
• Subjects: Amyloid - chemistry; amyloid fibril; Animals; lysozyme; Muramidase - chemistry; phenylalanine; Phenylalanine - chemistry; protein; Protein Folding; Protein Structure, Secondary; Raman spectroscopy; Spectrum Analysis, Raman; structure; Ultraviolet Rays
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/bip.20330

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. © 2005 Wiley Periodicals, Inc. Biopolymers 79: 58–61, 2005 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [e-mail]