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Thermodynamics

The world is flat

Nature Chemical Biology volume 6, pages 312–313 (2010)Cite this article

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NMR-measured order parameters of methyl groups can be used to quantify the entropy of protein conformational change associated with calmodulin–peptide ligand interactions. This conformational entropy is a major contributor to the affinity of calmodulin interactions and can now be determined experimentally on a per-atom basis.

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Figure 1: Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I (CaMKI).

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Authors and Affiliations

  1. Harald Schwalbe and Jörg Rinnenthal are at the Center for Biomolecular Magnetic Resonance, Institute of Organic Chemistry and Chemical Biology, Deutsche Forschungsgemeinschaft Cluster of Excellence: Macromolecular Complexes, Johann Wolfgang Goethe-University Frankfurt, Frankfurt am Main, Germany.,

    Harald Schwalbe & Jörg Rinnenthal

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  1. Harald Schwalbe
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  2. Jörg Rinnenthal
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Correspondence to Harald Schwalbe.

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The authors declare no competing financial interests.

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Schwalbe, H., Rinnenthal, J. The world is flat. Nat Chem Biol 6, 312–313 (2010). https://doi.org/10.1038/nchembio.357

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