13C cross-polarization/magic angle spinning NMR studies of α-elastin preparations show retention of overall structure and reduction of mobility with a decreased number of cross-links

• Published in: Biopolymers Vol. 59; no. 4; pp. 266 - 275
• Main Authors: Kumashiro, Kristin K., Kim, Minna S., Kaczmarek, Sylvia E., Sandberg, Lawrence B., Boyd, Charles D.
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 05.10.2001
• Subjects: aorta; copper deficiency; cross-linked peptides; high-resolution solid-state 13C NMR; undercross-linked peptides; α-elastin
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/1097-0282(20011005)59:4<266::AID-BIP1023>3.0.CO;2-2

High‐resolution solid‐state 13C NMR spectra are presented for samples of α‐elastin prepared from the aorta of normal and copper‐deficient pigs. Chemical shifts of the various peaks indicate that both the normal and undercross‐linked peptides have similar overall structures. However, 13C T1, 13C T1ρ, and 1H T1ρ measurements indicate that the α‐elastin peptides obtained from the abnormal elastic fibers samples exhibit altered mobilities, particularly in their side chains. Results from spectra taken with a range of contact times and from dipolar dephasing experiments are consistent with conclusions reached with the relaxation measurements. Namely, the loss of function associated with the undercross‐linked sample is correlated to a small but measurable difference in relative mobility. © 2001 John Wiley & Sons, Inc. Biopolymers 59: 266–275, 2001