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Int. J. Mol. Sci. 2012, 13(8), 10368-10386; doi:10.3390/ijms130810368
Review

Macromolecule-Assisted de novo Protein Folding

1,2,* , 2
, 2
, 3,*  and 1,2,*
Received: 26 July 2012; in revised form: 14 August 2012 / Accepted: 17 August 2012 / Published: 20 August 2012
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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Abstract: In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, although all these macromolecules have been known to effectively and robustly solubilize their linked heterologous proteins in fusion or display technology. Thus, their roles in the aggregation of linked endogenous polypeptides need to be elucidated and incorporated into the mechanisms of de novo protein folding in vivo. In the classic hydrophobic interaction-based stabilizing mechanism underlying the molecular chaperone-assisted protein folding, it has been assumed that the macromolecules connected through a simple linkage without hydrophobic interactions and conformational changes would make no effect on the aggregation of their linked polypeptide chains. However, an increasing line of evidence indicates that the intrinsic properties of soluble macromolecules, especially their surface charges and excluded volume, could be important and universal factors for stabilizing their linked polypeptides against aggregation. Taken together, these macromolecules could act as folding helpers by keeping their linked nascent chains in a folding-competent state. The folding assistance provided by these macromolecules in the linkage context would give new insights into de novo protein folding inside the cell.
Keywords: folding; macromolecules; aggregation; hydrophobic interaction; molecular chaperone; surface charges; excluded volume folding; macromolecules; aggregation; hydrophobic interaction; molecular chaperone; surface charges; excluded volume
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Choi, S.I.; Son, A.; Lim, K.-H.; Jeong, H.; Seong, B.L. Macromolecule-Assisted de novo Protein Folding. Int. J. Mol. Sci. 2012, 13, 10368-10386.

AMA Style

Choi SI, Son A, Lim K-H, Jeong H, Seong BL. Macromolecule-Assisted de novo Protein Folding. International Journal of Molecular Sciences. 2012; 13(8):10368-10386.

Chicago/Turabian Style

Choi, Seong Il; Son, Ahyun; Lim, Keo-Heun; Jeong, Hotcherl; Seong, Baik L. 2012. "Macromolecule-Assisted de novo Protein Folding." Int. J. Mol. Sci. 13, no. 8: 10368-10386.


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