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Default NMR study of collagen-water interactions.

NMR study of collagen-water interactions.

Related Articles NMR study of collagen-water interactions.

Biopolymers. 1994 Dec;34(12):1615-26

Authors: Renou JP, Bonnet M, Bielicki G, Rochdi A, Gatellier P

A proton magnetic resonance study of different cross-linked collagens was performed as a function of water content and temperature. Collagens from three connective tissues (calf, steer, and cow) were chosen according to the different number of nonreducible multivalent cross-links, which increases during the life of animal. Samples were hydrated under five well-defined water activities (Aw) ranging from 0.44 to 0.85. The transverse and cross-relaxation times of water protons were studied as a function of temperature from -20 up to 100 degrees C. From the temperature dependence of relaxation rates, the dynamics of water molecules can be described according to different processes: exchange of protons at the higher temperatures and dipole-dipole interactions that prevail at the lower temperatures. The exchange processes are analyzed as a function of the residence lifetime of water molecules at the protein interface and of the transfer of spin energy from water protons to macromolecule protons. The proton dipole-dipole interactions are related to the relaxation parameters of protein and water protons. All the relaxation parameters showed specific behavior for the 0.44 water activity for every tissue. The collagen tissue from calf also showed distinct behavior in comparison with other tissues.

PMID: 7849224 [PubMed - indexed for MEDLINE]



Source: PubMed
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