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

The protein‐folding mechanism remains a major puzzle in life science. Purified soluble activation‐induced cytidine deaminase (AID) is one of the most difficult proteins to obtain. Starting from inclusion bodies containing a C‐terminally truncated version of AID (residues 1–153; AID153), an optimized...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2017-12, Vol.73 (12), p.955-969
Hauptverfasser:	Lee, Schuyler, Wang, Chao, Liu, Haolin, Xiong, Jian, Jiji, Renee, Hong, Xia, Yan, Xiaoxue, Chen, Zhangguo, Hammel, Michal, Wang, Yang, Dai, Shaodong, Wang, Jing, Jiang, Chengyu, Zhang, Gongyi
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation-induced cytidine deaminase Asparagine BASIC BIOLOGICAL SCIENCES Bonding cis/trans-proline Crystals Cytidine deaminase Cytidine Deaminase - chemistry Denaturation Folding Humans Hydrogen Bonding Hydrogen bonds Hydrophobicity Inclusion bodies Isomerization pH effects Point mutation Proline Proline - chemistry Protein Conformation Protein Denaturation Protein Folding Proteins Research Papers Residues
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