期刊
SCIENCE
卷 342, 期 6159, 页码 741-743出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1239764
关键词
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资金
- European Research Council [310080]
- Agence National de la Recherche [ANR-12-BS10-009-01]
- Spanish Ministerio de Economia y Competitividad [BES-2010-031186]
- STSM COST Action [TD1002-10006]
- European Research Council (ERC) [310080] Funding Source: European Research Council (ERC)
The mechanical unfolding of the muscle protein titin by atomic force microscopy was a landmark in our understanding of single-biomolecule mechanics. Molecular dynamics simulations offered atomic-level descriptions of the forced unfolding. However, experiment and simulation could not be directly compared because they differed in pulling velocity by orders of magnitude. We have developed high-speed force spectroscopy to unfold titin at velocities reached by simulation (similar to 4 millimeters per second). We found that a small beta-strand pair of an immunoglobulin domain dynamically unfolds and refolds, buffering pulling forces up to similar to 100 piconewtons. The distance to the unfolding transition barrier is larger than previously estimated but is in better agreement with atomistic predictions. The ability to directly compare experiment and simulation is likely to be important in studies of biomechanical processes.
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