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Cooperativity in macromolecular assembly

Nature Chemical Biology volume 4, pages 458–465 (2008)Cite this article

Abstract

The thermodynamic principle of cooperativity is used to drive the formation of specific macromolecular complexes during the assembly of a macromolecular machine. Understanding cooperativity provides insight into the mechanisms that govern assembly and disassembly of multicomponent complexes. Our understanding of assembly mechanisms is lagging considerably behind our understanding of the structure and function of these complexes. A significant challenge remains in tackling the thermodynamics and kinetics of the intermolecular interactions required for all cellular functions.

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Figure 1: Thermodynamic cycles and cooperativity.
Figure 2: Mechanisms of cooperativity.
Figure 3: Physical models for assembly.
Figure 4: Cooperativity in Notch signaling.
Figure 5: Cooperativity in 30S ribosome assembly.
Figure 6: Kinetic traps, cofactors and chaperones.

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Acknowledgements

The author thanks S. Edgcomb for helpful discussions and critical reading of the manuscript, S. Blacklow for critical comments and E. Vogel of Leonardo's Basement for the photo of the large Soma cube. This work was supported by a grant from the US National Institutes of Health (GM-53757 to J.R.W.).

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  1. James R. Williamson is in the Departments of Molecular Biology and Chemistry, and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA. jrwill@scripps.edu,

    James R Williamson

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Williamson, J. Cooperativity in macromolecular assembly. Nat Chem Biol 4, 458–465 (2008). https://doi.org/10.1038/nchembio.102

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