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Redistribution and loss of side chain entropy upon formation of a calmodulin–peptide complex

Nature Structural Biology volume 7, pages 72–77 (2000)Cite this article

Abstract

The response of the internal dynamics of calcium-saturated calmodulin to the formation of a complex with a peptide model of the calmodulin-binding domain of the smooth muscle myosin light chain kinase has been studied using NMR relaxation methods. The backbone of calmodulin is found to be unaffected by the binding of the domain, whereas the dynamics of side chains are significantly perturbed. The changes in dynamics are interpreted in terms of a heterogeneous partitioning between structure (enthalpy) and dynamics (entropy). These data provide a microscopic view of the residual entropy of a protein in two functional states and suggest extensive enthalpy/entropy exchange during the formation of a protein–protein interface.

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Figure 1: Illustration of various motions affecting the obtained generalized order parameters for methyl deuterons.
Figure 2: Methyl symmetry axis order parameters (S2axis) for methyl groups in CaM.
Figure 3: Differences in order parameters (bound - free) in CaM.
Figure 4: Color-coded representation of the side chain dynamics of calmodulin.
Figure 5: Effective correlation times (τe) for methionine methyl groups in a, CaM and b, the CaM–smMLCKp complex.

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Acknowledgements

We thank K. Sharp and J. Kranz for helpful discussions. This work was supported by a grant and a postdoctoral fellowship from the National Institutes of Health.

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  1. Department of Biochemistry and Biophysics, The Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, 19104, Pennsylvania, USA

    Andrew L. Lee, Sandra A. Kinnear & A. Joshua Wand

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Correspondence to A. Joshua Wand.

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Lee, A., Kinnear, S. & Wand, A. Redistribution and loss of side chain entropy upon formation of a calmodulin–peptide complex. Nat Struct Mol Biol 7, 72–77 (2000). https://doi.org/10.1038/71280

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