Backbone assignment of crystalline E. coli maltose binding protein.

Autor: Schubeis T; Centre de Résonance Magnétique Nucléaire à Très Hauts champs (UMR 5082, CNRS/Ecole Normale Supérieure de Lyon/Université Claude Bernard Lyon 1), Université de Lyon, 5 rue de la Doua, 69100, Villeurbanne, France., Stanek J; Faculty of Chemistry, University of Warsaw, Żwirki i Wigury 101, 02089, Warsaw, Poland., Pintacuda G; Centre de Résonance Magnétique Nucléaire à Très Hauts champs (UMR 5082, CNRS/Ecole Normale Supérieure de Lyon/Université Claude Bernard Lyon 1), Université de Lyon, 5 rue de la Doua, 69100, Villeurbanne, France. guido.pintacuda@ens-lyon.fr.
Jazyk: angličtina
Zdroj: Biomolecular NMR assignments [Biomol NMR Assign] 2021 Oct; Vol. 15 (2), pp. 317-322. Date of Electronic Publication: 2021 Apr 16.
DOI: 10.1007/s12104-021-10023-w
Abstrakt: The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets. Here, we report virtually complete (~ 90%) backbone resonance assignments obtained on a microcrystalline sample of MBP with 1 H-detected solid-state NMR at fast (> 100 kHz) magic-angle spinning. We additionally present the detailed description of the methodology employed for the preparation of the sample and the acquisition and analysis of the NMR spectra. The chemical shifts, obtained with a single uniformly 15 N,  13 C-labelled and fully-protonated sample and about 2 weeks on a 800 MHz NMR spectrometer, have been deposited to the BMRB under the accession number 50089.
(© 2021. The Author(s), under exclusive licence to Springer Nature B.V.)
Databáze: MEDLINE
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