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accessHydrogen bonds are a primary driving force for de novo protein folding. Corrigendum
aDepartment of Biomedical Research, National Jewish Health, Denver, CO 80206, USA, bDepartment of Immunology and Microbiology, School of Medicine, University of Colorado Denver, Aurora, CO 80206, USA, cDepartment of Chemistry, University of Missouri, Columbus, Mississippi, USA, dPhysical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, and eDepartment of Biochemistry and Molecular Biology, Peking Union Medical College, Beijing 100005, People's Republic of China
*Correspondence e-mail: chengyujiang@gmail.com, zhangg@njhealth.org
The paper by Lee et al. [(2017). Acta Cryst. D73, 955–969] is withdrawn.
Keywords: hydrogen bonds; cis/trans-proline; protein folding; corrigendum.
We wish to withdraw the paper by Lee et al. (2017![[Lee, S., Wang, C., Liu, H., Xiong, J., Jiji, R., Hong, X., Yan, X., Chen, Z., Hammel, M., Wang, Y., Dai, S., Wang, J., Jiang, C. & Zhang, G. (2017). Acta Cryst. D73, 955-969.]](../../../../../../logos/arrows/d_arr.gif "Lee, S., Wang, C., Liu, H., Xiong, J., Jiji, R., Hong, X., Yan, X., Chen, Z., Hammel, M., Wang, Y., Dai, S., Wang, J., Jiang, C. & Zhang, G. (2017). Acta Cryst. D73, 955-969.")
) on the of a protein believed to have been AID (activation-induced cytidine deaminase). It has subsequently been shown that the crystal studied was of E. coli RNA-binding protein Hfq, a contaminant in the protein preparation. The associated PDB entry, 5w09, has also been made obsolete. Our conclusions regarding the critical role of proline residues in protein folding, successful folding of proteins at high pH, and hydrogen bonds as a driving force in de novo protein folding are not affected, and further details will be published elsewhere.
References
Lee, S., Wang, C., Liu, H., Xiong, J., Jiji, R., Hong, X., Yan, X., Chen, Z., Hammel, M., Wang, Y., Dai, S., Wang, J., Jiang, C. & Zhang, G. (2017). Acta Cryst. D73, 955–969. CrossRef IUCr Journals Google Scholar
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