Khatri , Bhavesh and Raghunathan, S and Chakraborti, S and Rahisuddin, R. and Kumaran, S. and Tadala, R and Wagh, P and Priyakumar, U.D. and Chatterjee, J (2021) Desolvation of Peptide Bond by O to S Substitution Impacts Protein Stability. Angewandte. International Edition.
Full text not available from this repository. (Request a copy)Abstract
Amino acid side chains are key to fine-tuning the microenvironment polarity in proteins composed of polar amide bonds. Here, we report that substituting an oxygen atom of the backbone amide bond with sulfur atom desolvates the thioamide bond, thereby increasing its lipophilicity. The impact of such local desolvation by O to S substitution in proteins was tested by synthesizing thioamidated variants of Pin1 WW domain. We observe that a thioamide acts in synergy with nonpolar amino acid side chains to reduce the microenvironment polarity and increase protein stability by more than 14 °C. Through favorable van der Waals and hydrogen bonding interactions, this single atom substitution significantly stabilizes proteins without altering the amino acid sequence and structure of the native protein.
| Item Type: | Article |
|---|---|
| Additional Information: | The Copyright of this article belongs to WILEY |
| Uncontrolled Keywords: | HDT; host epigentic machinery; host-pathogen interaction;host transcription factors; tuberculosis |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 18 Apr 2022 06:20 |
| Last Modified: | 18 Apr 2022 06:20 |
| URI: | http://crdd.osdd.net/open/id/eprint/2952 |
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