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Trimethylsilyl tag for probing protein-ligand interactions by NMR

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Authors

Becker, Walter
Adams, Luke A
Graham, Bim
Wagner, Gabriel E
Zangger, Klaus
Otting, Gottfried
Nitsche, Christoph

Journal Title

Journal ISSN

Volume Title

Publisher

Springer (part of Springer Nature): Springer Open Choice Hybrid Journals

Abstract

Protein-ligand titrations can readily be monitored with a trimethylsilyl (TMS) tag. Owing to the intensity, narrow line shape and unique chemical shift of a TMS group, dissociation constants can be determined from straightforward 1D 1H-NMR spectra not only in the fast but also in the slow exchange limit. The tag is easily attached to cysteine residues and a sensitive reporter of ligand binding also at sites where it does not interfere with ligand binding or catalytic efficiency of the target protein. Its utility is demonstrated for the Zika virus NS2B-NS3 protease and the human prolyl isomerase FK506 binding protein.

Description

Citation

Source

Journal of biomolecular NMR

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Access Statement

Open Access

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Restricted until

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