Journal article
Reversible Mechanical Unfolding of Single Ubiquitin Molecules
Biophysical journal, v 87(6), pp 3995-4006
Dec 2004
PMID: 15361414
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Single-molecule manipulation techniques have enabled the characterization of the unfolding and refolding process of individual protein molecules, using mechanical forces to initiate the unfolding transition. Experimental and computational results following this approach have shed new light on the mechanisms of the mechanical functions of proteins involved in several cellular processes, as well as revealed new information on the protein folding/unfolding free-energy landscapes. To investigate how protein molecules of different folds respond to a stretching force, and to elucidate the effects of solution conditions on the mechanical stability of a protein, we synthesized polymers of the protein ubiquitin and characterized the force-induced unfolding and refolding of individual ubiquitin molecules using an atomic-force-microscope-based single-molecule manipulation technique. The ubiquitin molecule was highly resistant to a stretching force, and the mechanical unfolding process was reversible. A model calculation based on the hydrogen-bonding pattern in the native structure was performed to explain the origin of this high mechanical stability. Furthermore, pH effects were studied and it was found that the forces required to unfold the protein remained constant within a pH range around the neutral value, and forces decreased as the solution pH was lowered to more acidic values.
Metrics
Details
- Title
- Reversible Mechanical Unfolding of Single Ubiquitin Molecules
- Creators
- Chia-Lin Chyan - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanFan-Chi Lin - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanHaibo Peng - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanJian-Min Yuan - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanChung-Hung Chang - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanSheng-Hsien Lin - Department of Chemistry, National Dong Hwa University, Hualien, TaiwanGuoliang Yang - Department of Chemistry, National Dong Hwa University, Hualien, Taiwan
- Publication Details
- Biophysical journal, v 87(6), pp 3995-4006
- Publisher
- Biophysical Society
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Physics
- Web of Science ID
- WOS:000225426700035
- Scopus ID
- 2-s2.0-10044290957
- Other Identifier
- 991014878267004721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biophysics