C-13 cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links
Kk. Kumashiro et al., C-13 cross-polarization/magic angle spinning NMR studies of alpha-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links, BIOPOLYMERS, 59(4), 2001, pp. 266-275
High-resolution solid-state C-13 NMR spectra are presented for samples of a
-elastin prepared from the aorta of normal and copper-deficient pigs. Chemi
cal shifts of the various peaks indicate that both the normal and undercros
s-linked peptides have similar overall structures. However, C-13 T-1, C-13
T-1p, and H-1 T-1p measurements indicate that the alpha -elastin peptides o
btained from the abnormal elastic fibers samples exhibit altered mobilities
, particularly in their side chains. Results from spectra taken with a rang
e of contact times and from dipolar dephasing experiments are consistent wi
th conclusions reached with the relaxation measurements. Namely, the loss o
f junction associated with the undercross-linked sample is correlated to a
small but measurable difference in relative mobility. (C) 2001 John Wiley &
Sons, Inc.