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Updated: Oct 1, 2026

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
Published on: October 9, 2021
Secondary and tertiary structure of nucleotide-binding domain of alphasubunit of Na+/K+-ATPase
Katerina Hofbauerová1, Vladimír Kopecký, Rüdiger Ettrich
1Department of Physical and Macromolecular Chemistry, Charles University, Albertov 2030, CZ-128 40 Prague 2, Czech Republic. hofbauer@biomed.cas.cz
Abstract:
The nucleotide-binding domain of the alpha subunit of mouse brain Na+/K+-ATPase was expressed and isolated from Escherichia coli cells. A model structure was constructed by comparative modeling with and without docked ATP. This was compared with the secondary structure determination from UV circular dichroism and Raman spectroscopy. Thus, we support the quality of the model and the correct folding of the recombinant protein. ATP binding was followed by Raman difference spectroscopy, and its influence on the secondary structure of the N domain seems to not be significant.
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