Literature DB >> 29652265

Hydrogen bonds are a primary driving force for de novo protein folding. Corrigendum.

Schuyler Lee1, Chao Wang1, Haolin Liu1, Jian Xiong2, Renee Jiji2, Xia Hong1, Xiaoxue Yan1, Zhangguo Chen3, Michal Hammel4, Yang Wang1, Shaodong Dai1, Jing Wang3, Chengyu Jiang5, Gongyi Zhang1.   

Abstract

The paper by Lee et al. [(2017). Acta Cryst. D73, 955-969] is withdrawn.

Entities:  

Keywords:  cis/trans-proline; corrigendum; hydrogen bonds; protein folding

Year:  2018        PMID: 29652265      PMCID: PMC5892881          DOI: 10.1107/S2059798318004047

Source DB:  PubMed          Journal:  Acta Crystallogr D Struct Biol        ISSN: 2059-7983            Impact factor:   7.652


We wish to withdraw the paper by Lee et al. (2017 ▸) on the crystal structure 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.
  1 in total

1.  Hydrogen bonds are a primary driving force for de novo protein folding.

Authors:  Schuyler Lee; Chao Wang; Haolin Liu; Jian Xiong; Renee Jiji; Xia Hong; Xiaoxue Yan; Zhangguo Chen; Michal Hammel; Yang Wang; Shaodong Dai; Jing Wang; Chengyu Jiang; Gongyi Zhang
Journal:  Acta Crystallogr D Struct Biol       Date:  2017-11-10       Impact factor: 7.652

  1 in total

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