Backbone and side-chain NMR resonance assignments of Ciona intestinalis[Formula: see text]-crystallin
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Updated: Nov 2, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Matthew D Jimenez1, Mina Mozafari1, Cat Tuong Nguyen Hoang1
1Department of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, 92697-2025, CA, United States of America.
Abstract:
The structural [Formula: see text]-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the [Formula: see text] crystallins of the vertebrate eye lens. Ci-[Formula: see text] maintains the metal cation-binding sites of ancestral crystallins while also sharing common structural motifs with vertebrate lens crystallins. Due to its structure and strong interaction with Ca[Formula: see text], Ci-[Formula: see text] is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding [Formula: see text] crystallins' evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-[Formula: see text] with TALOS-N predictions on the H[Formula: see text], H[Formula: see text], C[Formula: see text], C[Formula: see text] and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the [Formula: see text]-crystallin family.
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