Aromatic-Aromatic Interactions Drive Fold Switch of GA95 and GB95 with Three Residue Difference

IF 7.6 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Chen Chen, Zeting Zhang, Mojie Duan, Qiong Wu, Minghui Yang, Ling Jiang, Maili Liu, Conggang Li
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引用次数: 0

Abstract

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.
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来源期刊
Chemical Science
Chemical Science CHEMISTRY, MULTIDISCIPLINARY-
CiteScore
14.40
自引率
4.80%
发文量
1352
审稿时长
2.1 months
期刊介绍: Chemical Science is a journal that encompasses various disciplines within the chemical sciences. Its scope includes publishing ground-breaking research with significant implications for its respective field, as well as appealing to a wider audience in related areas. To be considered for publication, articles must showcase innovative and original advances in their field of study and be presented in a manner that is understandable to scientists from diverse backgrounds. However, the journal generally does not publish highly specialized research.
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