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High-Speed Force Spectroscopy Unfolds Titin at the Velocity of Molecular Dynamics Simulations.

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Title: High-Speed Force Spectroscopy Unfolds Titin at the Velocity of Molecular Dynamics Simulations.
Authors: Rico, Felix, Gonzalez, Laura, Casuso, Ignacio, Puig-Vidal, Manel, Scheuring, Simon
Source: Science (pre-March 2025). 11/8/2013, Vol. 342 Issue 6159, preceding p741-743. 4p.
Subjects: Spectrum analysis, Denaturation of proteins, Molecular dynamics, Muscle proteins, Connectin, Atomic force microscopy
Abstract: 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 (~4 millimeters per second). We found that a small b-strand pair of an immunoglobulin domain dynamically unfolds and refolds, buffering pulling forces up 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. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: High-Speed Force Spectroscopy Unfolds Titin at the Velocity of Molecular Dynamics Simulations.
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  Data: <searchLink fieldCode="AR" term="%22Rico%2C+Felix%22">Rico, Felix</searchLink><br /><searchLink fieldCode="AR" term="%22Gonzalez%2C+Laura%22">Gonzalez, Laura</searchLink><br /><searchLink fieldCode="AR" term="%22Casuso%2C+Ignacio%22">Casuso, Ignacio</searchLink><br /><searchLink fieldCode="AR" term="%22Puig-Vidal%2C+Manel%22">Puig-Vidal, Manel</searchLink><br /><searchLink fieldCode="AR" term="%22Scheuring%2C+Simon%22">Scheuring, Simon</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 11/8/2013, Vol. 342 Issue 6159, preceding p741-743. 4p.
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  Data: <searchLink fieldCode="DE" term="%22Spectrum+analysis%22">Spectrum analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Denaturation+of+proteins%22">Denaturation of proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink><br /><searchLink fieldCode="DE" term="%22Muscle+proteins%22">Muscle proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Connectin%22">Connectin</searchLink><br /><searchLink fieldCode="DE" term="%22Atomic+force+microscopy%22">Atomic force microscopy</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: 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 (~4 millimeters per second). We found that a small b-strand pair of an immunoglobulin domain dynamically unfolds and refolds, buffering pulling forces up 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. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=91882214
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        Value: 10.1126/science.1239764
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        Text: English
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      – SubjectFull: Molecular dynamics
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      – SubjectFull: Muscle proteins
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      – SubjectFull: Atomic force microscopy
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              Text: 11/8/2013
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