Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-63-2021
https://doi.org/10.5194/mr-2-63-2021
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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Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2020-37', Stewart Loh, 28 Jan 2021
    • AC1: 'Comment on mr-2020-37', Kevin Gardner, 10 Feb 2021
  • RC2: 'Comment on mr-2020-37', Walter Chazin, 28 Jan 2021
    • AC1: 'Comment on mr-2020-37', Kevin Gardner, 10 Feb 2021
  • RC3: 'Comment on mr-2020-37', Anonymous Referee #3, 29 Jan 2021
    • AC1: 'Comment on mr-2020-37', Kevin Gardner, 10 Feb 2021
  • AC1: 'Comment on mr-2020-37', Kevin Gardner, 10 Feb 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Kevin Gardner on behalf of the Authors (22 Feb 2021)  Author's response    Manuscript
ED: Publish as is (23 Feb 2021) by Rolf Boelens
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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.