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Eisenmesser, E. Z., Millet, O., Labeikovsky, W., Korzhnev, D. M., Wolf-Watz, M., Bosco, D. A., Skalicky, J. J., Kay, L. E., & Kern, D. (2005). Intrinsic dynamics of an enzyme underlies catalysis. Nature, 438(7064), 117–121.

Authors 9
  1. Elan Z. Eisenmesser (first)
  2. Oscar Millet (additional)
  3. Wladimir Labeikovsky (additional)
  4. Dmitry M. Korzhnev (additional)
  5. Magnus Wolf-Watz (additional)
  6. Daryl A. Bosco (additional)
  7. Jack J. Skalicky (additional)
  8. Lewis E. Kay (additional)
  9. Dorothee Kern (additional)
References 30 Referenced 1,000
  1. Jencks, W. P. Catalysis in Chemistry and Enzymology (Dover, New York, 1987) / Catalysis in Chemistry and Enzymology by WP Jencks (1987)
  2. Hammes, G. Multiple conformational changes in enzyme catalysis. Biochemistry 41, 8221–8228 (2002) (10.1021/bi0260839) / Biochemistry by G Hammes (2002)
  3. Benkovic, S. J. & Hammes-Schiffer, S. A perspective on enzyme catalysis. Science 301, 1196–1202 (2003) (10.1126/science.1085515) / Science by SJ Benkovic (2003)
  4. Garcia-Viloca, M., Gao, J., Karplus, M. & Truhlar, D. G. How enzymes work: analysis by modern rate theory and computer simulations. Science 303, 186–195 (2004) (10.1126/science.1088172) / Science by M Garcia-Viloca (2004)
  5. Eisenmesser, E. Z., Akke, M., Bosco, D. A. & Kern, D. Enzyme dynamics during catalysis. Science 295, 1520–1523 (2002) (10.1126/science.1066176) / Science by EZ Eisenmesser (2002)
  6. Austin, R. H. et al. Dynamics of ligand binding to myoglobin. Biochemistry 14, 5355–5373 (1975) (10.1021/bi00695a021) / Biochemistry by RH Austin (1975)
  7. Berendsen, H. J. C. & Hayward, S. Collective protein dynamics in relation to function. Curr. Opin. Struct. Biol. 10, 165–169 (2000) (10.1016/S0959-440X(00)00061-0) / Curr. Opin. Struct. Biol. by HJC Berendsen (2000)
  8. Rod, T. H., Radkiewicz, J. L. & Brooks, C. L. Correlated motion and the effect of distal mutations in dihydrofolate reductase. Proc. Natl Acad. Sci. USA 100, 6980–6985 (2003) (10.1073/pnas.1230801100) / Proc. Natl Acad. Sci. USA by TH Rod (2003)
  9. Suel, G. M., Lockless, S. W., Wall, M. A. & Ranganathan, R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nature Struct. Biol. 10, 59–69 (2003) (10.1038/nsb881) / Nature Struct. Biol. by GM Suel (2003)
  10. Agarwal, P. K., Geist, A. & Gorin, A. Protein dynamics and enzymatic catalysis: Investigating the peptidyl-prolyl cis-trans isomerization activity of cyclophilin A. Biochemistry 43, 10605–10618 (2004) (10.1021/bi0495228) / Biochemistry by PK Agarwal (2004)
  11. Schmid, F. X. Prolyl isomerases. Adv. Protein Chem. 59, 243–282 (2001) (10.1016/S0065-3233(01)59008-7) / Adv. Protein Chem. by FX Schmid (2001)
  12. Goff, S. P. Genetic control of retrovirus susceptibility in mammalian cells. Annu. Rev. Genet. 38, 61–85 (2004) (10.1146/annurev.genet.38.072902.094136) / Annu. Rev. Genet. by SP Goff (2004)
  13. Mulder, F. A. A., Mittermaier, A., Hon, B., Kahlquist, F. W. & Kay, L. E. Studying excited states of proteins by NMR spectroscopy. Nature Struct. Biol. 8, 932–935 (2001) (10.1038/nsb1101-932) / Nature Struct. Biol. by FAA Mulder (2001)
  14. Palmer, A. G. NMR characterization of the dynamics of biomacromolecules. Chem. Rev. 104, 3623–3640 (2004) (10.1021/cr030413t) / Chem. Rev. by AG Palmer (2004)
  15. Kern, D., Kern, G., Scherer, G., Fischer, G. & Drakenberg, T. Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy. Biochemistry 34, 13594–13602 (1995) (10.1021/bi00041a039) / Biochemistry by D Kern (1995)
  16. Zhao, Y. & Ke, H. Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Biochemistry 35, 7356–7361 (1996) (10.1021/bi9602775) / Biochemistry by Y Zhao (1996)
  17. Fischer, G., Bang, H. & Mech, C. Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides. Biomed. Biochim. Acta 43, 1101–1111 (1984) / Biomed. Biochim. Acta by G Fischer (1984)
  18. Ottiger, M., Zerbe, O., Guntert, P. & Wuthrich, K. The NMR solution conformation of unligated human cyclophilin A. J. Mol. Biol. 272, 64–81 (1997) (10.1006/jmbi.1997.1220) / J. Mol. Biol. by M Ottiger (1997)
  19. Skrynnikov, N. R., Dahlquist, F. W. & Kay, L. E. Reconstructing NMR spectra of ‘invisible’ excited protein states using HSQC and HMQC experiments. J. Am. Chem. Soc. 124, 12352–12360 (2002) (10.1021/ja0207089) / J. Am. Chem. Soc. by NR Skrynnikov (2002)
  20. Wishart, D. S., Sykes, B. D. & Richards, F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311–333 (1991) (10.1016/0022-2836(91)90214-Q) / J. Mol. Biol. by DS Wishart (1991)
  21. Rozovsky, S., Jogl, G., Tong, L. & McKermott, A. E. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics. J. Mol. Biol. 310, 271–280 (2001) (10.1006/jmbi.2001.4673) / J. Mol. Biol. by S Rozovsky (2001)
  22. Williams, J. C. & McDermott, A. E. Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated. Biochemistry 34, 8309–8319 (1995) (10.1021/bi00026a012) / Biochemistry by JC Williams (1995)
  23. Schnell, J. R., Dyson, H. J. & Wright, P. E. Structure, dynamics, and catalytic function of dihydrofolate reductase. Annu. Rev. Biophys. Biomol. Struct. 33, 119–140 (2004) (10.1146/annurev.biophys.33.110502.133613) / Annu. Rev. Biophys. Biomol. Struct. by JR Schnell (2004)
  24. McElheny, D., Schnell, J. R., Lansing, J. C., Dyson, H. J. & Wright, P. E. Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. Proc. Natl Acad. Sci. USA 102, 5032–5037 (2005) (10.1073/pnas.0500699102) / Proc. Natl Acad. Sci. USA by D McElheny (2005)
  25. Ishima, R., Freedberg, D. I., Wang, Y. X., Louis, J. M. & Torchia, D. A. Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Struct. Fold. Des. 7, 1047–1055 (1999) (10.1016/S0969-2126(99)80172-5) / Struct. Fold. Des. by R Ishima (1999)
  26. Cole, R. & Loria, J. P. Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072–6081 (2002) (10.1021/bi025655m) / Biochemistry by R Cole (2002)
  27. Volkman, B. F., Lipson, D., Wemmer, D. E. & Kern, D. Two-state allosteric behaviour in a single-domain signalling protein. Science 291, 2429–2433 (2001) (10.1126/science.291.5512.2429) / Science by BF Volkman (2001)
  28. Rosen, M. K. et al. Selective methyl group protonation of perdeuterated proteins. J. Mol. Biol. 263, 627–636 (1996) (10.1006/jmbi.1996.0603) / J. Mol. Biol. by MK Rosen (1996)
  29. Loria, J. P., Rance, M. & Palmer, A. G. A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15, 151–155 (1999) (10.1023/A:1008355631073) / J. Biomol. NMR by JP Loria (1999)
  30. Carver, J. P. & Richards, R. E. A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation. J. Magn. Reson. 6, 89–105 (1972) / J. Magn. Reson. by JP Carver (1972)
Dates
Type When
Created 19 years, 10 months ago (Nov. 2, 2005, 2:06 p.m.)
Deposited 2 years, 3 months ago (May 18, 2023, 1:49 p.m.)
Indexed 32 minutes ago (Sept. 2, 2025, 7:52 p.m.)
Issued 19 years, 10 months ago (Nov. 1, 2005)
Published 19 years, 10 months ago (Nov. 1, 2005)
Published Print 19 years, 10 months ago (Nov. 1, 2005)
Funders 0

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@article{Eisenmesser_2005, title={Intrinsic dynamics of an enzyme underlies catalysis}, volume={438}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature04105}, DOI={10.1038/nature04105}, number={7064}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Eisenmesser, Elan Z. and Millet, Oscar and Labeikovsky, Wladimir and Korzhnev, Dmitry M. and Wolf-Watz, Magnus and Bosco, Daryl A. and Skalicky, Jack J. and Kay, Lewis E. and Kern, Dorothee}, year={2005}, month=nov, pages={117–121} }