Biomolecules: Where the Physics of Complexity and Simplicity Meet

Hans Frauenfelder; Peter G. Wolynes

doi:10.1063/1.881414

Features

/

Article

Biomolecules: Where the Physics of Complexity and Simplicity Meet

FEB 01, 1994

How can a protein fold itself properly in on instant, and how could functional proteins possibly have evolved in the brief span of life on Earth? Addressing such questions, we learn a lot about the physics of complexity.

DOI: 10.1063/1.881414

Hans Frauenfelder

Peter G. Wolynes

Are we moving toward a time when no new and exciting problems appear in physics? Would the vaunted “theory of everything” mean the end of creative physics? A similar scenario was played out at the end of the last century, when some great physicists declared that only minor problems remained to be solved.

This article is only available in PDF format

References

1. See articles in Biologically Inspired Physics, L. Peliti, ed., Plenum, New York (1992),
and Spin Glasses and Biology, D. L. Stein, ed., World Scientific, Singapore (1992).
2. H. Frauenfelder, S. Sligar, P. G. Wolynes, Science 254, 1598 (1991). https://doi.org/SCIEAS
H. Frauenfelder, F. Parak, R. D. Young, Annu. Rev. Biophys. Chem. 17, 451 (1988).https://doi.org/ARBCEY
3. J. A. McCammon, S. C. Harvey, Dynamics of Proteins and Nucleic Acids, Cambridge U.P., New York (1987).
4. M. Mezard, G. Parisi, M. Virasoro, Spin Glass Theory and Beyond, World Scientific, Singapore (1987).
K. Binder, A. P. Young, Rev. Mod. Phys. 58, 8011 (1986).https://doi.org/RMPHAT
5. I. Ibsen et al., Phys. Rev. Lett. 62, 1916 (1989).https://doi.org/PRLTAO
6. B. Derrida, Phys. Rev. B 24, 2613 (1981); https://doi.org/PRBMDO
D. Gross, M. Mezard, Nucl. Phys. B 240, 431 (1984).https://doi.org/NUPBBO
7. J. D. Bryngelson, P. G. Wolynes, Proc. Natl. Acad. Sci. USA 84, 7524 (1987).https://doi.org/PNASA6
8. J. D. Bryngelson, P. G. Wolynes, J. Phys. Chem. 93, 6902 (1989). https://doi.org/JPCHAX
E. I. Shakhnovich, A. M. Gutin, Europhys. Lett. 9, 569 (1989).https://doi.org/EULEEJ
9. D. L. Stein, Proc. Natl. Acad. Sci. USA 82, 3670 (1985).https://doi.org/PNASA6
10. T. Garel, H. Orland, Europhys. Lett. 6, 307 (1988). https://doi.org/EULEEJ
E. I. Shakhnovich, A. M. Gutin, Europhys. Lett. 8, 327 (1989).https://doi.org/EULEEJ
11. N. Go, Annu. Rev. Biophys. Bioeng. 12, 183 (1983).https://doi.org/ABPBBK
12. P. Leopold, M. Montal, J. Onuchic, Proc. Natl. Acad. Sci. USA 89, 8721 (1992).https://doi.org/PNASA6
13. E. I. Shakhnovich, A. M. Gutin, Proc. Natl. Acad. Sci. USA 90, 7195 (1993); https://doi.org/PNASA6
E. I. Shakhnovich, A. M. Gutin, Protein Eng. 6, 793 (1993).https://doi.org/PRENE9
14. R. Goldstein, Z. Luthey‐Schulten, P. G. Wolynes, Proc. Natl. Acad. Sci. USA 87, 4918 (1992); https://doi.org/PNASA6
R. Goldstein, Z. Luthey‐Schulten, P. G. Wolynes, 89, 9029 (1992);
R. Goldstein, Z. Luthey‐Schulten, P. G. Wolynes, 90, 9949 (1993).
15. R. H. Austin, K. Beeson, L. Eisenstein, H. Frauenfelder, I. Gunsalus, Biochemistry 14, 5355 (1975).https://doi.org/BICHAW
16. J. Berendzen, D. Braunstein, Proc. Natl. Acad. Sci. USA 87, 1 (1990).
17. H. Frauenfelder, G. Petsko, D. Tsernoglou, Nature 280, 558 (1979).
18. W. Kohler, J. Friedrich, J. Chem. Phys. 90, 1270 (1989). https://doi.org/JCPSA6
R. Jankowich, G. J. Small, Science 237, 618 (1987).https://doi.org/SCIEAS
19. V. Goldanskii, Yu. F. Krupyanskii, V. N. Fleurov, Dokl. Akad. Nauk SSSR 272, 23 (1983).

More about the authors

Hans Frauenfelder, Los Alamos, National Laboratory, University of Illinois, Urbana‐Champaign.

Peter G. Wolynes, University of Illinois, Urbana‐Champaign.