ArticleChemical science2025
Aromatic-aromatic interactions drive fold switch of GA95 and GB95 with three residue difference.
Chen Chen, Zeting Zhang, Mojie Duan, Qiong Wu, Minghui Yang, Ling Jiang, Maili Liu, Conggang Li
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In one paragraphArticle in Chemical science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
Chen ChenKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.
Zeting ZhangKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.
Mojie DuanInterdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology Wuhan 430081 China mduan@wust.edu.cn.
Qiong WuKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.
Minghui YangKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.ORCID https://orcid.org/0000-0003-1067-2217 Ling JiangKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.
Maili LiuKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.ORCID https://orcid.org/0000-0002-9359-915X Conggang LiKey Laboratory of Magnetic Resonance in Biological Systems, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan, Wuhan National Laboratory for Optoelectronics, Wuhan Institute of Physics and Mathematics, Innovation Academy of Precision Measurement, Chinese Academy of Sciences Wuhan 430071 China conggangli@apm.ac.cn zhangzeting@wipm.ac.cn.ORCID https://orcid.org/0000-0002-5798-1722 Funding
No grant is acknowledged in the PubMed record.
6 · The paper itselfAbstract
Proteins typically adopt a single fold to carry out their function, but metamorphic proteins, with multiple folding states, defy this norm. Deciphering the mechanism of conformational interconversion of metamorphic proteins is challenging. Herein, we employed nuclear magnetic resonance (NMR), circular dichroism (CD), and all-atom molecular dynamics (MD) simulations to elucidate the mechanism of fold switching in proteins GA95 and GB95, which share 95% sequence homology. The results reveal that long-range interactions, especially aromatic π-π interactions involving residues F52, Y45, F30, and Y29, are critical for the protein switching from a 3α to a 4β + α fold. This study contributes to understanding how proteins with highly similar sequences fold into distinct conformations and may provide valuable insights into the protein folding code.
Identifiers
PMID39720130
PMCPMC11665817
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