Mechanical denaturation of globular protein in the solid state

A method for taking stress-strain diagrams in microsamples prepared from glutaraldehyde-treated monocrystals and amorphous films of hen egg-white lysozyme has been developed. Analysis of the diagrams has shown that the deformation obeys Hooke's law within 0–2%. Upon further deformation of a cry...

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Bibliographic Details
Published in:Biophysical chemistry 1987-12, Vol.28 (3), p.199-205
Main Authors: Gorelov, A.V., Morozov, V.N.
Format: Article
Language:English
Subjects:
Biological and medical sciences
chickens
Cross-linked crystal
Fundamental and applied biological sciences. Psychology
Lysozyme
Mechanical denaturation
Molecular biophysics
Physico-chemical properties of biomolecules
Stress-strain diagram
Ultimate strength
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Summary:A method for taking stress-strain diagrams in microsamples prepared from glutaraldehyde-treated monocrystals and amorphous films of hen egg-white lysozyme has been developed. Analysis of the diagrams has shown that the deformation obeys Hooke's law within 0–2%. Upon further deformation of a crystalline sample (up to 6–10%), when a critical stress, σ cr, is reached, the protein molecules in the sample denature and become greatly extended. Depending on the crystal type and crystallographic direction, the sample length increases 2–4 times. The critical stress is essentially dependent on the factors affecting intra- and intermolecular interactions: temperature, hydration level and urea concentration. Mechanisms for mechanical denaturation are proposed.
ISSN:0301-4622
1873-4200
DOI:10.1016/0301-4622(87)80090-X