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Nmr study of collagen‐water interactions
Author(s) -
Renou J. P.,
Bonnet M.,
Bielicki G.,
Rochdi A.,
Gatellier P.
Publication year - 1994
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360341206
Subject(s) - chemistry , proton , relaxation (psychology) , dipole , macromolecule , molecule , nuclear magnetic resonance , chemical physics , rotational correlation time , analytical chemistry (journal) , biophysics , chromatography , biochemistry , organic chemistry , psychology , social psychology , physics , quantum mechanics , biology
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 ( A w ) 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°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. © 1994 John Wiley & Sons, Inc.