Lysozyme fibrillation: Deep UV Raman spectroscopic characterization of protein structural transformation
Citations Over TimeTop 19% of 2005 papers
Abstract
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.
Related Papers
- → Palmitoyl Lysozyme-Induced Stabilization of PE (Phosphatidylethanolamine) Liposomes and Their Interaction with Candida albicans1(1995)10 cited
- → Regeneration to the Native Form of Hen Egg-White Lysozyme from Its Protected Derivatives(1978)6 cited
- 난백 lysozyme의 역가측정과 안정성에 관한 연구(1990)
- Stability studies of lysozyme for preformulation(2010)
- Lizozim kao prirodni prehrambeni konzervans(2014)