Allosteric regulation and catalysis emerge via a common route
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nchembio.98.pdf
Reference81 articles.
1. Monod, J., Wyman, J. & Changeux, J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88–118 (1965).
2. Kuriyan, J. & Eisenberg, D. The origin of protein interactions and allostery in colocalization. Nature 450, 983–990 (2007).
3. Boehr, D.D., McElheny, D., Dyson, H.J. & Wright, P.E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313, 1638–1642 (2006).
4. Loria, J.P., Berlow, R.B. & Watt, E.D. Characterization of enzyme motions by solution NMR relaxation dispersion. Acc. Chem. Res. 41, 214–221 (2008).
5. Watt, E.D., Shimada, H., Kovrigin, E.L. & Loria, J.P. The mechanism of rate-limiting motions in enzyme function. Proc. Natl. Acad. Sci. USA 104, 11981–11986 (2007).
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