ArticleChembiochem : a European journal of chemical biology2026
Quantifying Ligand-to-Protein Distances in Complex Environments Using Intermolecular
Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The determination of structural features is crucial to understand the interplay between structure and function of biomolecules and biomolecular complexes. In this context, nuclear magnetic resonance (NMR) spectroscopy provides experimental approaches, one of which is paramagnetic relaxation enhancement (PRE). Thus, placing a paramagnetic center and fluorine at strategic sites within (bio)molecules forming a complex enables the determination of distances through a straightforward, one-dimensionally guided NMR spectroscopic setup. Moreover, the almost absence of fluorine in biomolecules found in nature allows performing experimental work using cell-like or in cell conditions. Here, we made use of a single-cysteine mutant of Bacillus subtilis cold shock protein B (BsCspB) equipped with a paramagnetic spin label in complex with a fluorine-labeled variant of singly stranded DNA ligand dT4 to acquire intermolecular,
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