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Protein dynamic studies move to a new time slot

Many proteins frequently undergo structural rearrangement to complete their functions. Ligand entry and binding are often associated with some degree of localized disorder. Indeed, low populations of disordered excited states may help drive such processes. Characterization of these states is vital to understanding the mechanisms of many biological functions.

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Figure 1: Ribbon diagram of the C-terminal domain of the L99A T4 lysozyme mutant (red) complexed with benzene (white).
Figure 2: The results of an AutoDock study using a grid encompassing the entire HIV-1 protease surface.

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Acknowledgements

The authors would like to thank B. Matthews and C. Hill for kindly allowing us to use their figures for illustrative purposes and the appropriate journals for permission to reproduce them, and Mark Rance for a fruitful discussion.

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Correspondence to John Cavanagh or Ronald A. Venters.

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Cavanagh, J., Venters, R. Protein dynamic studies move to a new time slot. Nat Struct Mol Biol 8, 912–914 (2001). https://doi.org/10.1038/nsb1101-912

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