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In vitro proton NMR study of collagen in human aortic wall
Author(s) -
Vinée Philippe,
Meurer Bernard,
Constantinesco André,
Kohlberger Bernd,
Hauenstein Karl Heinz,
Laubenberger Jörg
Publication year - 1993
Publication title -
magnetic resonance in medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.696
H-Index - 225
eISSN - 1522-2594
pISSN - 0740-3194
DOI - 10.1002/mrm.1910290303
Subject(s) - elastin , macromolecule , proton , nuclear magnetic resonance , chemistry , second moment of area , free induction decay , line (geometry) , solid state nuclear magnetic resonance , in vitro , molecular physics , biophysics , materials science , crystallography , physics , magnetic resonance imaging , biochemistry , spin echo , pathology , thermodynamics , geometry , medicine , mathematics , quantum mechanics , radiology , biology
The authors relate the findings in the 1 H solid state line shape (at 60 MHz) of human aortic walls ( n = 12) in native state and after histologically controlled selective lysis of collagen and elastin. An analysis of the line shape shows a composite free induction decay (FID) consisting of a low amplitude (3‐7%) fast decaying component ( T 2 = 20 us) and a slow decaying one ( T 2 > 1 ms). The fast component is identified as the protons of the collagen macromolecules. The second moment computed from the experimental fast component of the FID is in agreement with published studies examining the motional characteristics of collagen by multinuclear NMR employing spin labeling. A theoretical second moment is computed for the collagen macromolecular backbone from the atomic positions in the superhelix. Comparison with the observed experimental values allows determination of the step angle (29°) of the fast rotational motion of the collagen strands along their long axis.