Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Backbone hydrogen bonding interaction of the inactive isoform of type III antifreeze proteins studied by 1H/15N-HSQC spectra

  • Seo-Ree, Choi (Department of Chemistry and RINS, Gyeongsang National University) ;
  • Sung Kuk, Kim (Department of Chemistry and RINS, Gyeongsang National University) ;
  • Jaewon, Choi (Department of Chemistry and RINS, Gyeongsang National University) ;
  • Joon-Hwa, Lee (Department of Chemistry and RINS, Gyeongsang National University)
  • Received : 2022.11.30
  • Accepted : 2022.12.13
  • Published : 2022.12.20
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Abstract

Antifreeze proteins (AFPs) bind to the ice crystals and then are able to inhibit the freezing of body fluid at subzero temperatures. Type III AFPs are categorized into three subgroups, QAE1, QAE2, and SP isoforms, based on differences in their isoelectric points. We prepared the QAE2 (AFP11) and SP (AFP6) isoforms of the notched-fin eelpout AFP and their mutant constructs and determined their temperature gradients of amide proton chemical shifts (𝚫δ/𝚫T) using NMR. The nfeAFP11 (QAE2) has the distinct 𝚫δ/𝚫T pattern of the first 310 helix compared to the QAE1 isoforms. The nfeAFP6 (SP) has the deviated 𝚫δ/𝚫T values of many residues, indicating its backbone conformational distortion. The study suggests the distortion in the H-bonding interactions and backbone conformation that is important for TH activities.

Keywords

Acknowledgement

This work was supported by grants from the National Research Foundation of Korea (2020R1A2C1006909 and 2022R1A4A1021817) and the Samsung Science and Technology Foundation (SSTF-BA1701-10).

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