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Peer-reviewedCC BY-NCChemistry, an Asian journal

Subzero-Temperature NMR Observation of Protein Dynamics and Ligand Binding Enabled by Encapsulation Within Coordination Cages.

  • Risa Ebihara1
  • Takahiro Nakama1
  • Miri Tadokoro1
  • Maho Yagi-Utsumi2,3,4
  • Koichi Kato2,3,4
  • Makoto Fujita4,5
5 affiliations
  1. 1Department of Applied Chemistry, School of Engineering, The University of Tokyo, Kashiwa, Chiba, Japan.
  2. 2Exploratory Research Center on Life and Living Systems (ExCELLS), Okazaki, Aichi, Japan.
  3. 3Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi, Japan.
  4. 4Institute for Molecular Science (IMS), Okazaki, Aichi, Japan.
  5. 5Tokyo College, U-Tokyo Institutes for Advanced Study (UTIAS), The University of Tokyo, Kashiwa, Chiba, Japan.
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Abstract

Lowering temperatures provides an effective strategy for probing rapid protein dynamics. However, conventional nuclear magnetic resonance (NMR) measurements are usually limited to temperatures above 0°C due to water freezing and increasing rotational correlation times. In this study, we report subzero-temperature NMR analysis enabled by encapsulating a protein within spherical coordination cages. Spatial confinement within the metallo-cages stabilizes proteins by preventing aggregation, enabling multi-dimensional NMR measurements of a 20 kDa protein at temperatures as low as -30°C in low-viscosity acetone-water mixtures. Below 0°C, the NMR spectra of the protein revealed markedly slowed dynamics, resolving two distinct conformations as split signals. Furthermore, the subzero-temperature analysis enabled detection of exchangeable hydroxy protons that are unobservable at ambient temperatures. Saturation transfer difference (STD) NMR revealed binding of carbohydrate hydroxy groups to lysozyme, owing to the large apertures of the cages, which permit ligand diffusion while the cages stabilize proteins under subzero conditions. This cage confinement thus facilitates the study of rapid protein dynamics and ligand binding beyond the limits of conventional solution NMR.

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Cite

BibTeXRIS
BibTeX
@article{ebihara2026subzerotemperature,
  title = {{Subzero-Temperature NMR Observation of Protein Dynamics and Ligand Binding Enabled by Encapsulation Within Coordination Cages.}},
  author = {Risa Ebihara and Takahiro Nakama and Miri Tadokoro and Maho Yagi-Utsumi and Koichi Kato and Makoto Fujita},
  journal = {Chemistry, an Asian journal},
  year = {2026},
  month = oct,
  doi = {10.1002/asia.71029},
  url = {https://europepmc.org/article/MED/42957983},
  note = {CC BY-NC},
}
RIS
TY  - JOUR
TI  - Subzero-Temperature NMR Observation of Protein Dynamics and Ligand Binding Enabled by Encapsulation Within Coordination Cages.
AU  - Risa Ebihara
AU  - Takahiro Nakama
AU  - Miri Tadokoro
AU  - Maho Yagi-Utsumi
AU  - Koichi Kato
AU  - Makoto Fujita
PY  - 2026
DA  - 2026/10/29
JO  - Chemistry, an Asian journal
DO  - 10.1002/asia.71029
UR  - https://europepmc.org/article/MED/42957983
AB  - Lowering temperatures provides an effective strategy for probing rapid protein dynamics. However, conventional nuclear magnetic resonance (NMR) measurements are usually limited to temperatures above 0°C due to water freezing and increasing rotational correlation times. In this study, we report subzero-temperature NMR analysis enabled by encapsulating a protein within spherical coordination cages. Spatial confinement within the metallo-cages stabilizes proteins by preventing aggregation, enabling multi-dimensional NMR measurements of a 20 kDa protein at temperatures as low as -30°C in low-viscosity acetone-water mixtures. Below 0°C, the NMR spectra of the protein revealed markedly slowed dynamics, resolving two distinct conformations as split signals. Furthermore, the subzero-temperature analysis enabled detection of exchangeable hydroxy protons that are unobservable at ambient temperatures. Saturation transfer difference (STD) NMR revealed binding of carbohydrate hydroxy groups to lysozyme, owing to the large apertures of the cages, which permit ligand diffusion while the cages stabilize proteins under subzero conditions. This cage confinement thus facilitates the study of rapid protein dynamics and ligand binding beyond the limits of conventional solution NMR.
SN  - 1861-4728
SN  - 1861-471X
ER  -