Abstract
Proteins have a free energy landscape possessing a large number of energy valleys separated by energy mountains.1,2,3 Many, perhaps all, complex systems have a rugged free energy landscape, including glasses4, spin glasses5, evolution6,7, and neural nets.5,8 The energy valleys, or minima, are called conformational substates (CS) and correspond to different structures in a protein or structural glass. Recent work shows analogies between proteins and glasses: The connection is between a single protein molecule (not a protein ensemble) and a glass sample. At low temperatures a protein or a glass is caught in a single free energy valley or conformational substate. As temperature increases, a glass liquifies and a protein moves from CS to CS. If temperature is then lowered below a transition temperature, a protein or a glass is again caught in a single CS. Proteins like glasses experience metastability below a transition temperature. In addition, both proteins and glasses display slow relaxation processes with non-exponential time dependence and non-Arrhenius temperature dependence.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
R. H. Austin et al., Biochem. 14, 4355 (1975).
A. Ansari et al., Proc. Natl.Acad. Sci. USA 82, 5000 (1985).
A. Ansari et al., Biophys. Chem. 26, 337 (1987).
J. Jäckle, Rep. Prog. Phys. 49, 171 (1986).
M. Mezard, G. Parisi and M. A. Virasoro, Spin Glass Theory and Beyond, World Scientific, Singapore (1987).
P. W. Anderson, Proc. Natl. Acad. Sci. USA 80, 3386 (1983).
A. S. Perelson and S. A. Kauffman, Molecular Evolution on Rugged Landscapes: Proteins, RNA and the Immune System,Proc. IX, Santa Fe Institute, Santa Fe, NM, in press.
J. J. Hopfield, Proc. Natl. Acad. Sci. USA 79, 2554 (1982).
L. Stryer, Biochemistry, Freeman, San Francisco (1988).
H. Frauenfelder, F. Parak and R. D. Young, Ann. Rev. Biophys. Biophys. Chem. 17, 451 (1988).
M. K. Hong et al., submitted to Biophys. J..
H. Frauenfelder et al., J. Phys. Chem., in press.
R. G. Palmer, in Cooperative Dynamics in Complex Systems, H. Takayama, ed. Springer, New York (1989) pp. 118–127.
J. Kuriyan, S. Wilz, M. Karplus and G. A. Petsko, J. Mol. Biol. 192, 133 (1986).
P. Ormos et al., Proc. Natl. Acad. Sci. USA 85, 8492 (1988).
I. E. T. Iben et al., Phys. Rev. Lett. 62, 1916 (1989).
H. Frauenfelder et al., J. Phys. Chem., in press.
H. Hassler, Phys. Rev. Lett. 58, 767 (1987).
R. Zwanzig, Proc. Natl. Acad. Sci. USA 85, 2029 (1988).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer Science+Business Media New York
About this chapter
Cite this chapter
Young, R.D. (1990). Glassy Dynamics and Relaxation in Proteins. In: Campbell, I.A., Giovannella, C. (eds) Relaxation in Complex Systems and Related Topics. NATO ASI Series, vol 222. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2136-9_25
Download citation
DOI: https://doi.org/10.1007/978-1-4899-2136-9_25
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-2138-3
Online ISBN: 978-1-4899-2136-9
eBook Packages: Springer Book Archive