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

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

doi:10.1107/S2059798317015303

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

Journal Article · Fri Nov 10 00:00:00 EST 2017 · Acta Crystallographica. Section D. Structural Biology

DOI:https://doi.org/10.1107/S2059798317015303· OSTI ID:1409879

Lee, Schuyler; Wang, Chao; Liu, Haolin; Xiong, Jian; Jiji, Renee; Hong, Xia;

; Chen, Zhangguo; Hammel, Michal;

;

; Wang, Jing; Jiang, Chengyu; Zhang, Gongyi

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; AID ¹⁵³ ), an optimized in vitro folding procedure was derived to obtain large amounts of AID ¹⁵³ , which led to crystals with good quality and to final structural determination. Interestingly, it was found that the final refolding yield of the protein is proline residue-dependent. The difference in the distribution of cis and trans configurations of proline residues in the protein after complete denaturation is a major determining factor of the final yield. A point mutation of one of four proline residues to an asparagine led to a near-doubling of the yield of refolded protein after complete denaturation. It was concluded that the driving force behind protein folding could not overcome the cis -to- trans proline isomerization, or vice versa , during the protein-folding process. Furthermore, it was found that successful refolding of proteins optimally occurs at high pH values, which may mimic protein folding in vivo . It was found that high pH values could induce the polarization of peptide bonds, which may trigger the formation of protein secondary structures through hydrogen bonds. It is proposed that a hydrophobic environment coupled with negative charges is essential for protein folding. Combined with our earlier discoveries on protein-unfolding mechanisms, it is proposed that hydrogen bonds are a primary driving force for de novo protein folding.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC03-76SF00098; AC02-05CH11231

OSTI ID:: 1409879

Alternate ID(s):: OSTI ID: 1420134

Journal Information:: Acta Crystallographica. Section D. Structural Biology, Journal Name: Acta Crystallographica. Section D. Structural Biology Vol. 73 Journal Issue: 12; ISSN 2059-7983

Publisher:: International Union of Crystallography (IUCr)Copyright Statement

Country of Publication:: United Kingdom

Language:: English

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Cited by: 8 works

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59 BASIC BIOLOGICAL SCIENCES
hydrogen bonds
cis/trans-proline
protein folding

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

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