Abstract
Using the haem group of myoglobin as a probe in optical experiments makes it possible to study its conformational fluctuations in real time. Results of these experiments can be directly interpreted in terms of the structure of the potential energy surface of the protein. The current view is that proteins have rough energy landscapes comprising a large number of minima which represent conformational substates, and that these substates are hierarchically organized. Here, we show that the energy landscape is characterized by a number of discrete distributions of barrier heights each representing a tier within a hierarchy of conformational substates. Furthermore, we provide evidence that the energy surface is self-similar and offer suggestions for a characterization of the protein fluctuations.
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References
Frauenfelder, H., Petsko, G. & Tsernoglou, D., X-ray diffraction as a probe of protein structural dynamics. Nature 280, 558–563 (1979).
Frauenfelder, H. & Wolynes, P.G., Where the physics of complexity and simplicity meet. Physics Today 47, 58–64 (1994).
Frauenfelder, H., Sligar, S.G. & Wolynes, P.G. The energy landscapes and motions of proteins. Science 254, 1598–1603 (1991).
Ansari, A. et al. Protein states and proteinquakes. Proc. natn. Acad. Sci. U.S.A. 82, 5000–5004 (1985).
Zollfrank, J., Friedrich, J., Vanderkooi, J.M. & Fidy, J. Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Biophys. J. 59, 305–312 (1991).
Thorn Leeson, D. & Wiersma, D.A. Low-temperature protein dynamics studied by the long-lived stimulated photon echo. J. phys. Chem. 98, 3913–3916 (1994).
Jankowiak, R. & Small, G.J. Hole-burning spectroscopy and relaxation dynamics of amorphous solids at low temperatures. Science 237, 618–625 (1987).
Wiersma, D.A. & Duppen, K. Picosecond holographic-grating spectroscopy. Science 237, 1147–1154 (1987).
Narasimhan, L.R. et al. Probing organic glasses at low temperature with variable time scale optical dephasing measurements. Chem. Rev. 90, 439–457 (1990).
Friedrich, J. Hole burning spectroscopy and physics of proteins. Meth. Enzym. 246, 226–259 (1995).
Friedrich, J., Gafert, J., Zollfrank, J., Vanderkooi, J.M. & Fidy, J. Spectral hole burning and selection of conformational substates in chromoproteins. Proc. natn. Acad. Sci. U.S.A. 91, 1029–1033 (1994).
Gafert, J., Friedrich, J., Vanderkooi, J.M. & Fidy, J. Structural changes and internal fields in proteins: A hole-burning Stark effect study of horseradish peroxidase. J. phys. Chem. 99, 5523–5527 (1995).
Littau, K.A., Bai, Y.S. & Fayer, M.D. Time evolution of non-photochemical hole burning linewidths: Observation of spectral diffusion at long times. Chem. Phys. Lett. 159, 1–6 (1989).
Hu, P. & Walker, L.R. Spectral-diffusion decay in echo experiments. Phys. Rev. B 18, 1300–1305 (1978).
Bai, Y.S. & Fayer, M.D. Time scales and optical dephasing measurements: Investigation of dynamics in complex systems. Phys. Rev. B 39, 11066–11084 (1989).
Thorn-Leeson, D. & Wiersma, D.A. Real time observation of low-temperature protein motions. Phys. Rev. Lett. 74, 2138–2141 (1995).
Shibata, Y., Kurita, A. & T Non-Lorentzian hole shape induced by spectral diffusion in H2-protoporphyrin substituted myoglobin in Spectral Hole-Burning and Related Spectroscopies: Science and Applications (Optical Society of America, Washington). 15, 80–83 (1994).
Kurita, A., Shibata, Y. & Kushida, T. Two-level systems in myoglobin probed by non-Lorentzian hole broadening in a temperature-cycling experiment. Phys. Rev. Lett. 74, 4349–4352 (1995).
Meijers, H.C. & Wiersma, D.A. Low temperature dynamics in amorphous solids: A photon echo study. J. chem. Phys. 101, 6927–6943 (1994).
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Leeson, D., Wiersma, D. Looking into the energy landscape of myoglobin. Nat Struct Mol Biol 2, 848–851 (1995). https://doi.org/10.1038/nsb1095-848
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DOI: https://doi.org/10.1038/nsb1095-848
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