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- W2775762521 abstract "Author(s): Fisher, Kaitlin M. | Abstract: The newly identified cytokine Interleukin-33 (IL-33) is currently the focus of multiple investigations into targeting pernicious inflammatory disorders. This mediator of inflammation plays a prevalent role in chronic disorders such as asthma, rheumatoid arthritis, and progressive heart disease. To date, little has been done to characterize the biophysical properties of IL-33, leaving a void in our understanding of the mechanism of action of this important cytokine. The work presented here characterizes the full native landscape of IL-33, from classifying the folding route to understanding the dynamic behavior of the protein in the native basin. The folding of IL-33 progresses through an intermediate state whose formation is necessitated by the folding of a stable nucleus, a critical step in providing a stable scaffold for folding the frustrated functional binding region in the final folding step. Though these regions share similar contacts, similar structural elements, and similar geometry, the functional region of IL-33 folds differently, allowing for it to be responsive and malleable without unfolding the whole protein. To evaluate the malleability and responsiveness of the functional region in the native state, NMR analysis of the native state dynamics on multiple timescales was assessed. This set of experiments shows that the functional region displays significant conformational entropy and dynamic heterogeneity in comparison with the rest of the structure in the native state. Taken together, conserved frustration and functionality along the folding route and native basin ensemble is a prime example of the evolutionary pressure to balance the need for efficient folding and structural stability with the preservation of functionality. IL-33 is a protein that must engage a highly dynamic receptor, and in doing so must be highly dynamic itself. Increased dynamics that allow for the proper function necessitates the presence of a driving force, and in the case of IL-33, it is provided by conserved frustration in the functional region of IL-33 along both the folding pathway and within the native state ensemble" @default.
- W2775762521 created "2017-12-22" @default.
- W2775762521 creator A5038268050 @default.
- W2775762521 date "2015-01-01" @default.
- W2775762521 modified "2023-09-26" @default.
- W2775762521 title "The Native Landscape of the Cytokine Interleukin-33 : Exploring the Link Between Folding and Dynamics" @default.
- W2775762521 hasPublicationYear "2015" @default.
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