Peer-reviewedCC BY 4.0Biomolecular Nmr Assignments1 Nov 2026

Backbone and side-chain NMR resonance assignments of Ciona intestinalis\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin

Matthew D. Jimenez¹
Mina Mozafari¹
Cat Tuong Nguyen Hoang¹
Miram Ali Al-Botaif¹
Jeongwoo Ko¹
Rachel W. Martin^1,2,3

¹Department of Chemistry, University of California, Irvine, 1102 Natural Sciences 2, Irvine, 92697-2025 CA United States of America
²Department of Molecular Biology and Biochemistry, University of California, Irvine, McGaugh Hall, Irvine, 92697-3900 CA United States of America
³Department of Ophthalmology and Visual Sciences, Gavin Herbert Eye Institute, University of California, Irvine, CA 92617 Irvine, United States of America

Abstract

The structural \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} crystallins of the vertebrate eye lens. Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} 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\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}²⁺\end{document}, Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} crystallins’ evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} with TALOS-N predictions on the H\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_N\end{document}, H\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_α\end{document}, C\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_α\end{document}, C\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_β\end{document} and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin family.

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BibTeX RIS

BibTeX

@article{jimenez2026backbone,
  title = {{Backbone and side-chain NMR resonance assignments of Ciona intestinalis\documentclass[12pt]minimal \usepackageamsmath \usepackagewasysym \usepackageamsfonts \usepackageamssymb \usepackageamsbsy \usepackagemathrsfs \usepackageupgreek \setlength\oddsidemargin-69pt \begindocument$$\beta \gamma$$\enddocument-crystallin}},
  author = {Matthew D. Jimenez and Mina Mozafari and Cat Tuong Nguyen Hoang and Miram Ali Al-Botaif and Jeongwoo Ko and Rachel W. Martin},
  journal = {Biomolecular Nmr Assignments},
  year = {2026},
  month = nov,
  doi = {10.1007/s12104-026-10280-7},
  url = {https://doi.org/10.1007/s12104-026-10280-7},
  note = {CC BY 4.0},
}

RIS

TY  - JOUR
TI  - Backbone and side-chain NMR resonance assignments of Ciona intestinalis\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin
AU  - Matthew D. Jimenez
AU  - Mina Mozafari
AU  - Cat Tuong Nguyen Hoang
AU  - Miram Ali Al-Botaif
AU  - Jeongwoo Ko
AU  - Rachel W. Martin
PY  - 2026
DA  - 2026/11/01
JO  - Biomolecular Nmr Assignments
DO  - 10.1007/s12104-026-10280-7
UR  - https://doi.org/10.1007/s12104-026-10280-7
AB  - The structural \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} crystallins of the vertebrate eye lens. Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} 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\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}^2+\end{document}, Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} crystallins’ evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document} with TALOS-N predictions on the H\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_N\end{document}, H\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_α\end{document}, C\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_α\end{document}, C\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}_β\end{document} and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin family.
SN  - 1874-2718
SN  - 1874-270X
ER  -

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