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Updated: May 14, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Dehydration-Induced Motional Heterogeneity in Native Collagen Protein Probed by Solid-State NMR Spectroscopy
Bijaylaxmi Patra1,2, Neeraj Sinha1,2
1Centre of Biomedical Research, SGPGIMS Campus, Raebareli Road, Lucknow 226014, India.
Abstract:
Collagen, the most abundant protein in animals, is a key structural component of muscle and connective tissues. Its structural integrity is strongly influenced by interactions with water; however, the molecular mechanisms underlying these effects remain poorly understood. Here, we investigate dehydration-induced perturbations in collagen dynamics within the native bone extracellular matrix (ECM) using 13C solid-state Nuclear Magnetic Resonance (NMR) relaxation measurements (T1 and T2) and associated rotational correlation times. This residue-specific approach reveals distinct dynamic behavior of the aliphatic carbons of the Gly-Pro-Hyp triplet and alanine, collectively constituting ∼70% of type I collagen. The 13C correlation times (10-6-10-8 s) demonstrate pronounced motional heterogeneity: dehydration predominantly restricts hydroxyproline Cβ, whereas H/D-exchanged perturbs hydroxyproline Cα, Cβ, and Cγ, as well as glycine Cα. These findings establish 13C relaxation as a powerful tool for probing water-mediated collagen dynamics in native systems.
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