The complexities of fibrous proteins in their native states often preclude the use of high-resolution solid-state NMR spectroscopy, particularly those utilizing multiple dimensions. In this study, the application of solid-state 13 C− 1 H heteronuclear correlation spectroscopy with frequency-switched Lee−Goldburg decoupling (FSLG-HETCOR) to an unenriched sample of native elastin is reported. These 2D experiments on lyophilized and hydrated elastin illustrate that individual contributions to the overall profile in the aliphatic region of its 13 C spectrum may be resolved. As a result, details of side-chain packing in the hydrated and dehydrated elastin are elucidated. Generally, the HETCOR data show that the removal of water produces a compact state in this protein.
No takes yet. Share an insight, caveat, or question.
Ohgo et al. (2009) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: