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Multidomain proteins under force
- Source :
- Nanotechnology. 28:174003
- Publication Year :
- 2017
- Publisher :
- IOP Publishing, 2017.
-
Abstract
- Advancements in single-molecule force spectroscopy techniques such as atomic force microscopy and magnetic tweezers allow investigation of how domain folding under force can play a physiological role. Combining these techniques with protein engineering and HaloTag covalent attachment, we investigate similarities and differences between four model proteins: I10 and I91-two immunoglobulin-like domains from the muscle protein titin, and two α + β fold proteins-ubiquitin and protein L. These proteins show a different mechanical response and have unique extensions under force. Remarkably, when normalized to their contour length, the size of the unfolding and refolding steps as a function of force reduces to a single master curve. This curve can be described using standard models of polymer elasticity, explaining the entropic nature of the measured steps. We further validate our measurements with a simple energy landscape model, which combines protein folding with polymer physics and accounts for the complex nature of tandem domains under force. This model can become a useful tool to help in deciphering the complexity of multidomain proteins operating under force.
- Subjects :
- 0301 basic medicine
Protein Folding
Magnetic tweezers
Materials science
Entropy
Protein domain
Bioengineering
Microscopy, Atomic Force
Protein Engineering
Article
03 medical and health sciences
Protein Domains
Connectin
General Materials Science
Electrical and Electronic Engineering
biology
Ubiquitin
Mechanical Engineering
Force spectroscopy
Energy landscape
General Chemistry
Protein engineering
Recombinant Proteins
030104 developmental biology
Mechanics of Materials
biology.protein
Biophysics
Polymer physics
Titin
Protein folding
Subjects
Details
- ISSN :
- 13616528 and 09574484
- Volume :
- 28
- Database :
- OpenAIRE
- Journal :
- Nanotechnology
- Accession number :
- edsair.doi.dedup.....a76f9ccd46e5bf0f38210d3ddeb727a7