Temperature softening of a protein in single-molecule experiments
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
- Technical University of Munich
Abstract
Mechanical flexibility is crucial for the function of proteins. However, such material properties are not easily accessible experimentally. We used single-molecule force spectroscopy to study the stiffness of a single domain of Dictyostelium discoideum filamin (ddFLN4) in a temperature range from 5 degrees C to 37 degrees C. Analyzing the distributions of unfolding forces allowed us to extract transition barrier heights and positions of the underlying energy landscape. We found a marked narrowing of unfolding force distributions with increasing temperature. This narrowing reflects an increase in transition state position from 2.7 angstrom to 7.8 angstrom and thus a reduction of the molecular spring constant of the protein by a factor of 7. We suggest this temperature softening reflects a shift in the nature of the interactions responsible for mechanical stability from hydrogen bonds to hydrophobic interactions. This result has important consequences for all interpretations of protein mechanical studies if experimental results obtained at room temperature are to be transferred to physiological temperatures. (c) 2005 Elsevier Ltd. All rights reserved.
Details
Original language | English |
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Pages (from-to) | 497-503 |
Number of pages | 7 |
Journal | Journal of Molecular Biology |
Volume | 354 |
Issue number | 2 |
Publication status | Published - 25 Nov 2005 |
Peer-reviewed | Yes |
External IDs
Scopus | 27644473726 |
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ORCID | /0000-0002-6209-2364/work/142237656 |
Keywords
Keywords
- AFM, titin, filamin, flexibility, ATOMIC-FORCE MICROSCOPY, ENERGY LANDSCAPE ROUGHNESS, MECHANICAL STABILITY, TRANSITION-STATE, IMMUNOGLOBULIN DOMAINS, TITIN, SPECTROSCOPY, ELASTICITY, ADHESION, PATHWAY