Výsledky vyhledávání - "Öberg, C. T."

Designing interactions by control of protein–ligand complex conformation: tuning arginine–arene interaction geometry for enhanced electrostatic protein–ligand interactions† †Electronic supplementary information (ESI) available: Synthesis experimental procedures and physical data for compounds. Data processing and refinement statistics for the X-ray crystal structures, 2Fo–Fc electron density maps for 15, 16, 19, and 20 when in complex with galectin-3C, electron densities for the alternate positions of 20 compared to 16, 2Fo–Fc electron density maps for galectin-3 in complex and R144 and R186 interactions with 15, 16, 19, and 20, and copies of 1H NMR spectra for compounds 4, 5, 7, 9, 10, 11, 13, 14, 16, 17, 19–22. See DOI: 10.1039/c7sc04749e

Autor: Noresson, A.-L., Aurelius, O., Öberg, C. T., Engström, O., Sundin, A. P., Håkansson, M., Stenström, O., Akke, M., Logan, D. T., Leffler, H., Nilsson, U. J.

Publikováno v: Chemical Science

3-Benzamido-2-O-sulfo-galactosides can be designed to control protein conformation into forming entropically favourable galectin-3-arginine salt bridges with ligand sulfates.
We investigated galectin-3 binding to 3-benzamido-2-O-sulfo-galactosid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::acf088927b461decee2a2aa5d7b47c9c
http://europepmc.org/articles/PMC5883865

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