Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions
Abstract A technique for the measurement of the dynamic Young's modulus E and logarithmic decrement ???? of protein crystals and other microscopic samples by the resonance method modified to a microscale is described. Monoclinic crystals of horse hemoglobin and sperm whale myoglobin; triclinic...
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crwiley:10.1002/bip.1981.360200304 2024-06-23T07:56:58+00:00 Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions Morozov, V. N. Morozova, T. Ya. 1981 http://dx.doi.org/10.1002/bip.1981.360200304 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.1981.360200304 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.1981.360200304 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 20, issue 3, page 451-467 ISSN 0006-3525 1097-0282 journal-article 1981 crwiley https://doi.org/10.1002/bip.1981.360200304 2024-06-11T04:41:19Z Abstract A technique for the measurement of the dynamic Young's modulus E and logarithmic decrement ???? of protein crystals and other microscopic samples by the resonance method modified to a microscale is described. Monoclinic crystals of horse hemoglobin and sperm whale myoglobin; triclinic hen egg white lysozyme crystals, crosslinked by glutaraldehyde; and native and crosslinked needlelike lysozyme crystals were studied, as were amorphous protein films. The E of wet protein crystals is shown to be in the range (3–15) × 10 3 kg/cm 2 , ???? = 0.3–0.7. The crosslinking does not significantly affect the values. General elastic properties were analyzed for triclinic lysozyme crystals. No frequency dependence of E and ???? was found over the frequency range of 2.5–65 kHz. The temperature dependence was found to be characteristic for glassy polymers; the decrement of Young's modulus was −2.4 ± 0.1%/°C. The guanidine HCl denaturation caused a 1000‐fold decrease of E , its temperature dependence becoming similar to that of rubberlike materials. Studies of pH and salt effects showed E to be influenced by ionization of the acidic groups at pH 3–4.5. A humidity decrease from 100 to 30% caused a three‐ to fourfold increase of E and a decrease of ????. The final values of E = (40–60) × 10 3 kg/cm 2 and ???? ≃ 0.1 were the same for dry crystals and amorphous films, whether crosslinked or not. These values may be attributed to the protein globular material. Article in Journal/Newspaper Sperm whale Wiley Online Library Biopolymers 20 3 451 467 |
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English |
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Abstract A technique for the measurement of the dynamic Young's modulus E and logarithmic decrement ???? of protein crystals and other microscopic samples by the resonance method modified to a microscale is described. Monoclinic crystals of horse hemoglobin and sperm whale myoglobin; triclinic hen egg white lysozyme crystals, crosslinked by glutaraldehyde; and native and crosslinked needlelike lysozyme crystals were studied, as were amorphous protein films. The E of wet protein crystals is shown to be in the range (3–15) × 10 3 kg/cm 2 , ???? = 0.3–0.7. The crosslinking does not significantly affect the values. General elastic properties were analyzed for triclinic lysozyme crystals. No frequency dependence of E and ???? was found over the frequency range of 2.5–65 kHz. The temperature dependence was found to be characteristic for glassy polymers; the decrement of Young's modulus was −2.4 ± 0.1%/°C. The guanidine HCl denaturation caused a 1000‐fold decrease of E , its temperature dependence becoming similar to that of rubberlike materials. Studies of pH and salt effects showed E to be influenced by ionization of the acidic groups at pH 3–4.5. A humidity decrease from 100 to 30% caused a three‐ to fourfold increase of E and a decrease of ????. The final values of E = (40–60) × 10 3 kg/cm 2 and ???? ≃ 0.1 were the same for dry crystals and amorphous films, whether crosslinked or not. These values may be attributed to the protein globular material. |
format |
Article in Journal/Newspaper |
author |
Morozov, V. N. Morozova, T. Ya. |
spellingShingle |
Morozov, V. N. Morozova, T. Ya. Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
author_facet |
Morozov, V. N. Morozova, T. Ya. |
author_sort |
Morozov, V. N. |
title |
Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
title_short |
Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
title_full |
Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
title_fullStr |
Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
title_full_unstemmed |
Viscoelastic properties of protein crystals: Triclinic crystals of hen egg white lysozyme in different conditions |
title_sort |
viscoelastic properties of protein crystals: triclinic crystals of hen egg white lysozyme in different conditions |
publisher |
Wiley |
publishDate |
1981 |
url |
http://dx.doi.org/10.1002/bip.1981.360200304 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.1981.360200304 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.1981.360200304 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biopolymers volume 20, issue 3, page 451-467 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.1981.360200304 |
container_title |
Biopolymers |
container_volume |
20 |
container_issue |
3 |
container_start_page |
451 |
op_container_end_page |
467 |
_version_ |
1802650396773056512 |