Low‐temperature glass transition in proteins
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 incr...
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crwiley:10.1002/bip.360240909 2024-06-02T08:14:53+00:00 Low‐temperature glass transition in proteins Morozov, V. N. Gevorkian, S. G. 1985 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 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 24, issue 9, page 1785-1799 ISSN 0006-3525 1097-0282 journal-article 1985 crwiley https://doi.org/10.1002/bip.360240909 2024-05-03T10:41:27Z 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. Article in Journal/Newspaper Sperm whale Wiley Online Library Biopolymers 24 9 1785 1799 |
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English |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Morozov, V. N. Gevorkian, S. G. |
spellingShingle |
Morozov, V. N. Gevorkian, S. G. Low‐temperature glass transition in proteins |
author_facet |
Morozov, V. N. Gevorkian, S. G. |
author_sort |
Morozov, V. N. |
title |
Low‐temperature glass transition in proteins |
title_short |
Low‐temperature glass transition in proteins |
title_full |
Low‐temperature glass transition in proteins |
title_fullStr |
Low‐temperature glass transition in proteins |
title_full_unstemmed |
Low‐temperature glass transition in proteins |
title_sort |
low‐temperature glass transition in proteins |
publisher |
Wiley |
publishDate |
1985 |
url |
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 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biopolymers volume 24, issue 9, page 1785-1799 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.360240909 |
container_title |
Biopolymers |
container_volume |
24 |
container_issue |
9 |
container_start_page |
1785 |
op_container_end_page |
1799 |
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1800738894881226752 |