Conformational changes of recombinant Ca2+–ATPase studied by reaction‐induced infrared difference spectroscopy

What is it about?

Ca2+-ATPase expression in yeast and its purification were established in our laboratory and the quality of the recombinant protein characterised mainly with time-resolved infrared spectroscopy. While the specific activity of the recombinant protein preparation is lower than that obtained from rabbit muscle, the active portion of the recombinant enzyme performs the same conformational changes during Ca2+ pumping and has the same activity.

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Why is it important?

Quality control of recombinant protein is important. Infrared spectroscopy can assess the quality of the active portion of an enzyme (this publication) as well as the structure of the overall protein content (including a possible inactive fraction of the recombinant protein) of the preparation (C. Li, S. Kumar, C. Montigny, M. le Maire, A. Barth (2014), Analyst 139, 4231 - 4240, DOI: 10.1039/c4an00483c).