In vitro proton NMR study of collagen in human aortic wall.
The authors relate the findings in the 1H 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 (T2 approximately 20 microseconds) and a slow decaying one (T2 > 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 degrees) of the fast rotational motion of the collagen strands along their long axis.
Laboratoire de Biomécanique, CHU Hautepierre, Strasbourg, France.
P
P
Vinée
B
B
Meurer
A
A
Constantinesco
B
B
Kohlberger
K H
KH
Hauenstein
J
J
Laubenberger
D000368:Aged; D000369:Aged, 80 and over; D001011:Aorta / Q000033:anatomy & histology / Q000378:metabolism*; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D004549:Elastin / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D005260:Female; D005561:Formates / Q000494:pharmacology; D006801:Humans; D006859:Hydrogen; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008297:Male; D008875:Middle Aged; D012815:Signal Processing, Computer-Assisted; D014357:Trypsin / Q000494:pharmacology
D005561:Formates; D046911:Macromolecular Substances; C030544:formic acid; D006859:Hydrogen; D003094:Collagen; D004549:Elastin; D014357:Trypsin