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Updated: May 26, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
The effects of biological environments on the electron-relay functionality of tryptophan residues in proteins
Xiaohua Chen1, Hongjing Dai, Jilai Li
1School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030, China. chxh7@cqu.edu.cn
Abstract:
Clarifying the contribution of tryptophan (Trp) to electron-transfer (ET) processes in different protein surroundings can help to understand the effective pathway of ET in proteins. Interactions between Trp residues and protein microsurroundings involve intermolecular H-bonds, cation and π-electron clouds of aromatic rings, the secondary structure and π orbital of aromatic rings, and so on. Detailed analyses reveal that the microsurroundings play an important role in modulating the electron-relay function of Trp in proteins. Generally, microsurroundings with strong Lewis acidity inhibit electron hole transport through Trp residues. Systems with weak Lewis acidity finely tune the electron-relay ability of Trp in proteins, while those with strong Lewis basicity strongly enhance the electron-relay ability of Trp residues.
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