Elucidating Conformational Dynamics and Thermostability of Designed Aromatic Clusters by Using Protein Cages

Yuki Hishikawa, Hiroki Noya, Satoru Nagatoishi, Takashi Yoshidome, Basudev Maity, Kouhei Tsumoto, Satoshi Abe, Takafumi Ueno

研究成果: ジャーナルへの寄稿学術論文査読

2 被引用数 (Scopus)

抄録

Multiple aromatic residues assemble to form higher ordered structures known as “aromatic clusters” in proteins and play essential roles in biological systems. However, the stabilization mechanism and dynamic behavior of aromatic clusters remain unclear. This study describes designed aromatic interactions confined within a protein cage to reveal how aromatic clusters affect protein stability. The crystal structures and calorimetric measurements indicate that the formation of inter-subunit phenylalanine clusters enhance the interhelix interactions and increase the melting temperature. Theoretical calculations suggest that this is caused by the transformation of the T-shaped geometry into π-π stacking at high temperatures, and the hydration entropic gain. Thus, the isolated nanoenvironment in a protein cage allows reconstruction and detailed analysis of multiple clustering residues for elucidating the mechanisms of various biomolecular interactions in nature which can be applied to design of bionanomaterials.

本文言語英語
論文番号e202300488
ジャーナルChemistry - A European Journal
29
34
DOI
出版ステータス出版済み - 2023 6月 19

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