Dehydration-Induced Motional Heterogeneity in Native Collagen Protein Probed by Solid-State NMR Spectroscopy

Key Points

• The study aims to investigate how dehydration affects the dynamics of native collagen proteins using solid-state NMR spectroscopy.
• Utilized solid-state NMR spectroscopy to examine native collagen samples under varying dehydration conditions.
• Analyzed C relaxation to assess the water-mediated dynamics of collagen.
• Evaluated motional heterogeneity in the collagen structure.
• Dehydration significantly altered the C relaxation dynamics in collagen (p < 0.01).
• Identified increased motional heterogeneity in dehydrated states compared to hydrated states, suggesting changes in protein stability.
• Established correlation between water content and relaxation rates in native collagen.