Lella, Muralikrishna ; Mahalakshmi, Radhakrishnan (2013) Pro-Gly mediated conformational switch of mycobacteriophage D29 holin transmembrane domain I is lipid concentration driven Chemical Communications, 49 (83). p. 9594. ISSN 1359-7345
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Official URL: http://doi.org/10.1039/C3CC45058A
Related URL: http://dx.doi.org/10.1039/C3CC45058A
Abstract
Biophysical and spectroscopic analysis of synthetic transmembrane domain I (TM1) of mycobacteriophage D29 holin shows a lipid concentration dependent conformational switch from an α-helix to a β-sheet structure. The reversibility of this switch, upon change in the lipid-to-peptide ratio, requires a central Pro-Gly segment, and is abolished upon mutation to Ala-Ala or DPro-Gly.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Royal Society of Chemistry. |
| ID Code: | 136844 |
| Deposited On: | 20 Aug 2025 11:29 |
| Last Modified: | 20 Aug 2025 11:29 |
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