| Literature DB >> 12324438 |
Mukta Singh-Zocchi1, Jeungphill Hanne, Giovanni Zocchi.
Abstract
Globular proteins are peculiar solids that display both local stability of their conformation and the ability to undergo large cooperative changes of shape (conformational changes). If one forces a large deformation of the molecule, such that the structure is necessarily changed, it is not obvious whether the deformed globule can still remain a solid or whether it will melt. Is it possible to plastically deform a protein? Here we investigate this question with a micro-mechanical experiment on a small region (approximately 10 molecules) of a protein monolayer adsorbed on a rigid surface. For the two proteins studied, albumin and myoglobin, we observed that the molecules can be substantially deformed (approximately 1-2 nm deformation) by comparatively small stresses applied for sufficiently long times. The deformation is irreversible, and the protein remains in the solid state (i.e., displays a nonzero shear modulus). The dynamics of the deformation is approximately logarithmic in time, similar to creep in solids. These results show that globular proteins adsorbed on a surface can be plastically deformed.Entities:
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Year: 2002 PMID: 12324438 PMCID: PMC1302309 DOI: 10.1016/S0006-3495(02)73981-7
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033