The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments

Sahar Foroutannejad; Lydia L. Good; Changfan Lin; Zachariah I. Carter; Mahlet G. Tadesse; Aaron L. Lucius; Brian R. Crane; Rodrigo A. Maillard

doi:10.1038/s41467-023-36701-y

Nature Communications (Feb 2023)

The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments

Sahar Foroutannejad,
Lydia L. Good,
Changfan Lin,
Zachariah I. Carter,
Mahlet G. Tadesse,
Aaron L. Lucius,
Brian R. Crane,
Rodrigo A. Maillard

Affiliations

Sahar Foroutannejad: Department of Chemistry, Georgetown University
Lydia L. Good: Department of Chemistry, Georgetown University
Changfan Lin: Department of Chemistry & Chemical Biology, Cornell University
Zachariah I. Carter: Department of Chemistry, University of Alabama at Birmingham
Mahlet G. Tadesse: Department of Mathematics and Statistics, Georgetown University
Aaron L. Lucius: Department of Chemistry, University of Alabama at Birmingham
Brian R. Crane: Department of Chemistry & Chemical Biology, Cornell University
Rodrigo A. Maillard: Department of Chemistry, Georgetown University

DOI: https://doi.org/10.1038/s41467-023-36701-y
Journal volume & issue: Vol. 14, no. 1
pp. 1 – 15

Abstract

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Characterizing folding pathways of large proteins that bind complex cofactors is challenging. The authors use optical tweezers to study the 542-residue FAD-binding lightsensor protein dCRY, identifying several intermediates and cofactor binding steps, and dissecting the role of FAD moieties in folding.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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