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Issue 8, 2019
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Single-site labeling of histidine in proteins, on-demand reversibility, and traceless metal-free protein purification

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Abstract

A precision methodology distinguishes one His from all the nucleophilic residues and its multiple copies. An easy-to-operate C–N bond formation labels diverse proteins without adversely affecting their structure and function. The late-stage transformation allows installation of distinct probes. The chemically triggered reversibility enables traceless metal-free purification of proteins with a His-tag.

Graphical abstract: Single-site labeling of histidine in proteins, on-demand reversibility, and traceless metal-free protein purification

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Publication details

The article was received on 01 Nov 2018, accepted on 19 Dec 2018 and first published on 19 Dec 2018


Article type: Communication
DOI: 10.1039/C8CC08733D
Chem. Commun., 2019,55, 1100-1103

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    Single-site labeling of histidine in proteins, on-demand reversibility, and traceless metal-free protein purification

    P. N. Joshi and V. Rai, Chem. Commun., 2019, 55, 1100
    DOI: 10.1039/C8CC08733D

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