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The effects of macromolecular crowding on the mechanical stability of protein molecules
Journal article   Open access   Peer reviewed

The effects of macromolecular crowding on the mechanical stability of protein molecules

Jian-Min Yuan, Chia-Lin Chyan, Huan-Xiang Zhou, Tse-Yu Chung, Haibo Peng, Guanghui Ping and Guoliang Yang
Protein science, v 17(12), pp 2156-2166
Dec 2008
PMID: 18780817
url
https://doi.org/10.1110/ps.037325.108View
Published, Version of Record (VoR) Open

Abstract

single molecule dextran mechanical unfolding macromolecular crowding mechanical stability ubiquitin
Macromolecular crowding, a common phenomenon in the cellular environments, can significantly affect the thermodynamic and kinetic properties of proteins. A single-molecule method based on atomic force microscopy (AFM) was used to investigate the effects of macromolecular crowding on the forces required to unfold individual protein molecules. It was found that the mechanical stability of ubiquitin molecules was enhanced by macromolecular crowding from added dextran molecules. The average unfolding force increased from 210 pN in the absence of dextran to 234 pN in the presence of 300 g/L dextran at a pulling speed of 0.25 μm/sec. A theoretical model, accounting for the effects of macromolecular crowding on the native and transition states of the protein molecule by applying the scaled-particle theory, was used to quantitatively explain the crowding-induced increase in the unfolding force. The experimental results and interpretation presented could have wide implications for the many proteins that experience mechanical stresses and perform mechanical functions in the crowded environment of the cell.

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Web of Science research areas
Biochemistry & Molecular Biology
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