Abstract
Here, we review recent studies aimed at defining the importance of quaternary structure to a model oligomeric enzyme, dihydrodipicolinate synthase. This will illustrate the complementary and synergistic outcomes of coupling the techniques of analytical ultracentrifugation with enzyme kinetics, in vitro mutagenesis, macromolecular crystallography, small angle X-ray scattering, and molecular dynamics simulations, to demonstrate the role of subunit self-association in facilitating protein dynamics and enzyme function. This multitechnique approach has yielded new insights into the molecular evolution of protein quaternary structure.
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Soares Da Costa, T. P., Christensen, J. B., Desbois, S., Gordon, S. E., Gupta, R., Hogan, C. J., … Perugini, M. A. (2015). Quaternary Structure Analyses of an Essential Oligomeric Enzyme. In Methods in Enzymology (Vol. 562, pp. 205–223). Academic Press Inc. https://doi.org/10.1016/bs.mie.2015.06.020
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