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

doi:10.1103/PhysRevLett.62.1916

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, and R. D. Young

Phys. Rev. Lett. 62, 1916 – Published 17 April 1989

Abstract

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.

Received 16 June 1988

DOI:https://doi.org/10.1103/PhysRevLett.62.1916

Authors & Affiliations

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, and R. D. Young

Department of Physics, University of Illinois, 1110 West Green Street, Urbana, Illinois 61801
Physik Department, Technische Univresität München, D-8046 Garcihg, Federal Republic of Germany
Department of Physics, Illinois State University, Normal, Illinois 61761