The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments
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 foldi...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-36701-y |
| _version_ | 1797864069984681984 |
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| author | Sahar Foroutannejad Lydia L. Good Changfan Lin Zachariah I. Carter Mahlet G. Tadesse Aaron L. Lucius Brian R. Crane Rodrigo A. Maillard |
| author_facet | Sahar Foroutannejad Lydia L. Good Changfan Lin Zachariah I. Carter Mahlet G. Tadesse Aaron L. Lucius Brian R. Crane Rodrigo A. Maillard |
| author_sort | Sahar Foroutannejad |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-09T22:46:44Z |
| format | Article |
| id | doaj.art-30dd6d9302b84ee08c76dff6d29b567b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-09T22:46:44Z |
| publishDate | 2023-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-30dd6d9302b84ee08c76dff6d29b567b2023-03-22T11:49:06ZengNature PortfolioNature Communications2041-17232023-02-0114111510.1038/s41467-023-36701-yThe cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experimentsSahar Foroutannejad0Lydia L. Good1Changfan Lin2Zachariah I. Carter3Mahlet G. Tadesse4Aaron L. Lucius5Brian R. Crane6Rodrigo A. Maillard7Department of Chemistry, Georgetown UniversityDepartment of Chemistry, Georgetown UniversityDepartment of Chemistry & Chemical Biology, Cornell UniversityDepartment of Chemistry, University of Alabama at BirminghamDepartment of Mathematics and Statistics, Georgetown UniversityDepartment of Chemistry, University of Alabama at BirminghamDepartment of Chemistry & Chemical Biology, Cornell UniversityDepartment of Chemistry, Georgetown UniversityCharacterizing 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.https://doi.org/10.1038/s41467-023-36701-y |
| spellingShingle | Sahar Foroutannejad Lydia L. Good Changfan Lin Zachariah I. Carter Mahlet G. Tadesse Aaron L. Lucius Brian R. Crane Rodrigo A. Maillard The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments Nature Communications |
| title | The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments |
| title_full | The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments |
| title_fullStr | The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments |
| title_full_unstemmed | The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments |
| title_short | The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments |
| title_sort | cofactor dependent folding mechanism of drosophila cryptochrome revealed by single molecule pulling experiments |
| url | https://doi.org/10.1038/s41467-023-36701-y |
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