Amyloid fibril depositions are associated with many neurodegenerative diseases. The nucleation step of fibrillation remains poorly characterized as no experimental technique allows for direct monitoring of nucleus formation. A new method based on 2D-correlation deep UV resonance Raman spectroscopy was applied to probe directly all species at early stages of lysozyme fibrillation, establish the sequential order of highly correlated events, and characterize quantitatively the kinetics of nucleus formation.