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

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

doi:https://doi.org/10.5194/mr-2-63-2021

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:

Robert Kaptein Festschrift

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

Supplement

https://doi.org/10.5194/mr-2-63-2021-supplement

Data sets

Backbone chemical shift assignments of ARNT PAS-B in 8M urea Xu, X., Dikiy, I., Evans, M.R., Marcelino, L.P., Gardner, K.H. https://doi.org/10.13018/BMR50761

Backbone chemical shift assignments of ARNT PAS-B F444Q/F446A/Y456T in 8M urea Xu, X., Dikiy, I., Evans, M.R., Marcelino, L.P., Gardner, K.H. https://doi.org/10.13018/BMR50762

Backbone chemical shift assignments of ARNT PAS-B Y456T in 8M urea Xu, X., Dikiy, I., Evans, M.R., Marcelino, L.P., Gardner, K.H. https://doi.org/10.13018/BMR50763

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.