Abstract
The scientific background of this example is biochemistry. The activity of some enzymes is regulated by formation or cleavage of disulfide bonds near the protein surface. This can be catalyzed by a group of proteins known as thioredoxin. Comparison of primary structures reveals that there is no consensus motif present in most of the thioredoxin-regulated target enzymes. In order to identify potential proteins that could be targets for thioredoxin, one can investigate protein structure data. We just need to search for cysteine sulfur atoms that are no further than 3 Å apart and close to the surface. But how? This exercise uses Jmol, Surface Racer, AWK, and shell programming.
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© 2013 Springer-Verlag Berlin Heidelberg
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Wünschiers, R. (2013). Querying for Potential Redox-Regulated Enzymes. In: Computational Biology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-34749-8_21
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DOI: https://doi.org/10.1007/978-3-642-34749-8_21
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Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-34748-1
Online ISBN: 978-3-642-34749-8
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