Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force
| Autor: | J. P. Renn, Andres F. Oberhauser, John F. Marko, H. Bai, Sucharita Bhattacharyya, Dmitrii E. Makarov, Chengzhi He, Hongbin Li, Andreas T Matouschek |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Magnetic tweezers Protein Denaturation Protein Folding Materials science Protein Conformation Deformation dynamics lcsh:Medicine Microscopy Atomic Force Article 03 medical and health sciences 0302 clinical medicine Exponential growth Spectrin Polymer chemistry lcsh:Science Protein Unfolding Range (particle radiation) Multidisciplinary lcsh:R Energy landscape Transition state Exponential function 030104 developmental biology Reflection (mathematics) Chemical physics Thermodynamics lcsh:Q 030217 neurology & neurosurgery |
| Zdroj: | Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019) Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | We investigated the mechanical unfolding of single spectrin molecules over a broad range of loading rates and thus unfolding forces by combining magnetic tweezers with atomic force microscopy. We find that the mean unfolding force increases logarithmically with loading rate at low loading rates, but the increase slows at loading rates above 1pN/s. This behavior indicates an unfolding rate that increases exponentially with the applied force at low forces, as expected on the basis of one-dimensional models of protein unfolding. At higher forces, however, the increase of the unfolding rate with the force becomes faster than exponential, which may indicate anti-Hammond behavior where the structures of the folded and transition states become more different as their free energies become more similar. Such behavior is rarely observed and can be explained by either a change in the unfolding pathway or as a reflection of a multidimensional energy landscape of proteins under force. |
| Databáze: | OpenAIRE |
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