Structural Analysis of Soluble Elastin in Dry and Hydrated States Using 13C Solid-State NMR
Tetsuo Asakura, Akira Naito, Keiichi Miyamoto
TL;DR
This study uses NMR to analyze how water affects the structure of soluble elastin, revealing conformational changes in dry and hydrated states.
Contribution
The novel contribution is the structural analysis of soluble elastin in both dry and hydrated states using 13C solid-state NMR.
Findings
Cross-linked alanine residues in dry soluble elastin show α-helix and random coil structures.
Hydrated soluble elastin favors random coil structures with some distorted helices.
Re-cross-linked elastin retains α-helix and random coil structures in dry and hydrated states.
Abstract
Elastin is the principal protein found in the elastic fibers of vertebrate tissues, and the water within these fibers plays a crucial role in preserving the structure and function of this hydrophobic protein. Soluble elastin was successfully obtained by repeatedly treating insoluble elastin, extracted from pig aorta, with oxalic acid. Solid-state NMR analysis was performed on the soluble elastin, focusing on conformation-dependent chemical shifts of alanine residues. This analysis revealed that cross-linked alanine residues exhibited both α-helix and random coil structures in the dry state. In contrast, the hydrated state favored random coil structures, with some distorted helices possibly present, indicating that the cross-linked configuration is relatively unstable. Similar conformational changes were observed in insoluble elastin, mirroring those found in the soluble form.…
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Taxonomy
TopicsConnective tissue disorders research · Protein Tyrosine Phosphatases · Galectins and Cancer Biology