Bajaj, Manish and Muddassir, Mohd and Choi, Bumjoon and Singh, Priyanka and Park, Jong Bum and Singh, Surjeet and Yadav, Manisha and Kumar, Rajesh and Eom, Kilho and Sharma, Deepak (2023) Single-molecule analysis of osmolyte-mediated nanomechanical unfolding behavior of a protein domain. International journal of biological macromolecules, 253. ISSN 1879-0003
Full text not available from this repository. (Request a copy)Abstract
The small organic molecules, known as osmolytes being ubiquitously present in different cell types, affect protein folding, stability and aggregation. However, it is unknown how the osmolytes affect the nanomechanical unfolding behavior of protein domain. Here, we show the osmolyte-dependent mechanical unfolding properties of protein titin immunoglobulin-27 (I27) domain using an atomic force microscopy (AFM)-based single-molecule force spectroscopy. We found that amines and methylamines improved the mechanical stability of I27 domain, whereas polyols had no effect. Interestingly, glycine betaine (GB) or trimethylamine-N-oxide (TMAO) increased the average unfolding force of the protein domain. The kinetic parameters analyzed at single-molecule level reveal that stabilizing effect of osmolytes is due to a decrease in the unfolding rate constant of I27, which was confirmed by molecular dynamics simulations. Our study reveals different effects that diverse osmolytes have on the mechanical properties of the protein, and suggests the potential use of osmolytes in modulating the mechanical stability of proteins required for various nano-biotechnological applications.
| Item Type: | Article |
|---|---|
| Additional Information: | The copyright of this article belongs to Elsevier Science |
| Uncontrolled Keywords: | Mechanical stability; Protein unfolding; Single-molecule force spectroscopy. |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 16 Jul 2024 02:08 |
| Last Modified: | 16 Jul 2024 02:08 |
| URI: | http://crdd.osdd.net/open/id/eprint/3162 |
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