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Unraveling the complexity of Exendin-4 folding through two distinct pathways.
- Source :
-
Journal of Mathematical Chemistry . Feb2024, Vol. 62 Issue 2, p356-366. 11p. - Publication Year :
- 2024
-
Abstract
- Protein folding is a prominent area of research in the life sciences. Exendin-4, a 39-amino acid peptide hormone, is of particular interest due to its potential therapeutic applications. In this study, we employed a steered molecular dynamics method to investigate the folding of Exendin-4. Our simulations reveal an intermediate state during the folding process, suggesting a more complex three-state mode of folding. Structural analysis indicates that Exendin-4 folds through two distinct pathways: pathway 1 involves gradual growth of a helical structure after the collapse of the hydrophobic core in the Trp-cage, while pathway 2 involves initial formation of local microdomains (helical structure and Trp-cage) which then combine with each other to form a stable native structure. We found that the folding along these pathways follows the hydrophobic collapse mechanism and the diffusion-collision mechanism, respectively. We believe that these two mechanisms together govern the folding of Exendin-4. These results significantly differ from those observed in most small protein folding. Our study on the folding of Exendin-4 will advance our understanding of the protein folding mechanism. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02599791
- Volume :
- 62
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Journal of Mathematical Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 174918647
- Full Text :
- https://doi.org/10.1007/s10910-023-01535-y