Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 2, issue 1
Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-63-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-63-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Articles | Volume 2, issue 1
Research article
 | 
10 Mar 2021
Research article |  | 10 Mar 2021

Fragile protein folds: sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations

Xingjian Xu, Igor Dikiy, Matthew R. Evans, Leandro P. Marcelino, and Kevin H. Gardner

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Latest update: 13 Dec 2024
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Short summary
While most proteins adopt one conformation, several interconvert between two or more very different structures. Knowing how sequence changes and small-molecule binding can control this behavior is essential for both understanding biology and inspiring new “molecular switches” which can control cellular pathways. This work contributes by examining these topics in the ARNT protein, showing that features of both the folded and unfolded states contribute to the interconversion process.
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