Detection of Labile Conformations of Elastin’s Prolines by Solid-State Nuclear Magnetic Resonance and Fourier Transform Infrared Techniques
2019
Dabalos, Chester L. | Ohgo, Kosuke | Kumashiro, Kristin K.
Samples of native elastin are prepared with high levels of enrichment at its prolines, which are believed to play a major role in the elasticity of elastin. Major and minor populations of trans and cis isomers at the Xaa-Pro imide bonds are detected in two-dimensional ¹³C nuclear magnetic resonance (NMR) experiments. One- and two-dimensional ¹³C NMR and isotope-edited Fourier transform infrared experiments are also used to identify the prolines’ folded and unfolded states, type II β-turn and random coil, respectively, at physiological temperatures. This study provides new details about elastin’s conformational ensemble. In addition, the cis–trans isomerization of its abundant prolines provides an additional mechanism of fiber elongation in tissue.
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