Outside Back Cover: Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering (Angew. Chem. 29/2025)

Ning Ding, Yaoyukun Jiang, Robbie Ge, Qianzhen Shao, Wook Shin, Xinchun Ran, Zhongyue J. Yang
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引用次数: 0

Abstract

The cover art symbolizes the transformation of the mesophilic amylase psA (red) into its cold-adapted variant psA121 (cyan) through computational linker engineering. The central swirling motif reflects a shift in temperature adaptation, driven by increased interdomain separation between the catalytic domain and the carbohydrate-binding module. This visual captures how a simple change in linker sequence enables enhanced enzymatic activity at low temperatures by modifying the conformational dynamics of bidomain enzyme amylase, as described by Zhongyue J. Yang et al. in their Research Article (e202505991).

Abstract Image

外封底:利用高通量计算工程增强biddomain淀粉酶的冷适应性[j]。化学29/2025)
封面艺术象征着通过计算机连接工程将中温淀粉酶psA(红色)转化为其冷适应变体psA121(青色)。中心旋转基序反映了温度适应的转变,这是由催化结构域和碳水化合物结合模块之间的结构域间分离增加所驱动的。正如Zhongyue J. Yang等人在他们的研究文章(e202505991)中所描述的那样,这幅图捕捉到了连接子序列的简单改变如何通过改变双结构域淀粉酶的构象动力学来增强低温下的酶活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Angewandte Chemie
Angewandte Chemie 化学科学, 有机化学, 有机合成
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