Low‐temperature glass transition in proteins

• Published in: Biopolymers
• Main Authors: Morozov, V. N., Gevorkian, S. G.
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1985
• Subjects: Sperm whale
• Online Access: http://dx.doi.org/10.1002/bip.360240909; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360240909; https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360240909

Abstract The viscoelastic properties of solid samples (crystals, amorphous films) of hen egg white lysozyme, bovine serum albumin, and sperm whale myoglobin were studied in the temperature range of 100–300 K at different hydration levels. Decreasing the temperature was shown to cause a steplike increase in the Young's modulus of highly hydrated protein samples (with water content exceeding 0.3 g/g dry weight of protein) in the temperature range of 237–251 K, followed by a large increase in the modulus in the broad temperature interval of 240–130 K, which we refer to as a mechanical glass transition. Soaking the samples in 50% glycerol solution completely removed the steplike transition without significantly affecting the glass transition. The apparent activation energy determined from the frequency dependence of the glass‐transition temperature was found to be 18 kcal/mol for wet lysozyme crystals. Lowering the humidity causes both the change of the Young's modulus in response to the transition and the activation energy to decrease. The thermal expansion coefficient of amorphous protein films also indicates the glass transition at 150–170 K. The data presented suggest that the glass transition in hydrated samples is located in the surface layer of proteins and related to the immobilization of the protein groups and strongly bound water.