Glassy behavior of a protein

I. E.T. Iben, D. Braunstein, W. Doster, H. Frauenfelder, M. K. Hong, J. B. Johnson, S. Luck, P. Ormos, A. Schulte, P. J. Steinbach, A. H. Xie, R. D. Young

Research output: Article

356 Citations (Scopus)


Quasistatic and kinetic studies of the infrared CO stretch bands of carbonmonoxymyoglobin show that proteins and glasses share essential characteristics, in particular metastability below a transition temperature and relaxation processes that are nonexponential in time and non-Arrhenius in temperature.

Original languageEnglish
Pages (from-to)1916-1919
Number of pages4
JournalPhysical review letters
Issue number16
Publication statusPublished - jan. 1 1989

ASJC Scopus subject areas

  • Physics and Astronomy(all)

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    Iben, I. E. T., Braunstein, D., Doster, W., Frauenfelder, H., Hong, M. K., Johnson, J. B., Luck, S., Ormos, P., Schulte, A., Steinbach, P. J., Xie, A. H., & Young, R. D. (1989). Glassy behavior of a protein. Physical review letters, 62(16), 1916-1919.