Tammo Diercks

TL;DR: As a novel approach for studying carbohydrate-lectin interactions spectroscopically, the resolution and specificity of (19)F-detected NMR spectroscopy with the sensitivity of the saturation transfer difference (STD) technique are combined.

TL;DR: The crystal structure of PRL-1 in complex with the Bateman module of CNNM2 (CNNM2BAT), which consists of two cystathionine β-synthase (CBS) domains and represents an intracellular regulatory module of the transporter, sheds new light on the structural basis underlying the interaction between PRL phosphatases and CNNM transporters.

TL;DR: The results of the present study suggest that the T568I mutation exerts its pathogenic effect in humans by constraining the conformational equilibrium of the CBS module of CNNM2, which becomes 'locked' in its flat form.

TL;DR: 3D models of the interacting complexes have been proposed based on the analysis of glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells by using NMR.

TL;DR: A new 2D STD-TOCSYreF experiment is presented here that enables comprehensive epitope mapping of fluorinated glycans by combining the spectral resolution of 19 F with the spatial resolution and coverage of 1 H.