Literature DB >> 12012438

Secondary and tertiary structure of nucleotide-binding domain of alphasubunit of Na+/K+-ATPase.

Katerina Hofbauerová1, Vladimír Kopecký, Rüdiger Ettrich, Olga Ettrichová, Evzen Amler.   

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. Copyright 2002 Wiley Periodicals, Inc.

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Year:  2002        PMID: 12012438     DOI: 10.1002/bip.10093

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  1 in total

1.  Limitations in linearized analyses of binding equilibria: binding of TNP-ATP to the H4-H5 loop of Na/K-ATPase.

Authors:  M Kubala; J Plásek; E Amler
Journal:  Eur Biophys J       Date:  2003-03-06       Impact factor: 1.733

  1 in total

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