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Chaperoning Roles of Macromolecules Interacting with Proteins in Vivo

by 1,2,*, 2 and 1,2,*
1
Translational Research Center for Protein Function Control, Yonsei University, Seoul 120-749, Korea
2
Department of Biotechnology, College of Bioscience and Biotechnology, Yonsei University, Seoul 120-749, Korea
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2011, 12(3), 1979-1990; https://doi.org/10.3390/ijms12031979
Received: 28 January 2011 / Revised: 15 February 2011 / Accepted: 17 March 2011 / Published: 18 March 2011
(This article belongs to the Section Molecular Recognition)
The principles obtained from studies on molecular chaperones have provided explanations for the assisted protein folding in vivo. However, the majority of proteins can fold without the assistance of the known molecular chaperones, and little attention has been paid to the potential chaperoning roles of other macromolecules. During protein biogenesis and folding, newly synthesized polypeptide chains interact with a variety of macromolecules, including ribosomes, RNAs, cytoskeleton, lipid bilayer, proteolytic system, etc. In general, the hydrophobic interactions between molecular chaperones and their substrates have been widely believed to be mainly responsible for the substrate stabilization against aggregation. Emerging evidence now indicates that other features of macromolecules such as their surface charges, probably resulting in electrostatic repulsions, and steric hindrance, could play a key role in the stabilization of their linked proteins against aggregation. Such stabilizing mechanisms are expected to give new insights into our understanding of the chaperoning functions for de novo protein folding. In this review, we will discuss the possible chaperoning roles of these macromolecules in de novo folding, based on their charge and steric features. View Full-Text
Keywords: molecular chaperones; macromolecules; hydrophobic interactions; stabilization; aggregation; surface charges; steric hindrance; de novo folding molecular chaperones; macromolecules; hydrophobic interactions; stabilization; aggregation; surface charges; steric hindrance; de novo folding
MDPI and ACS Style

Choi, S.I.; Lim, K.-H.; Seong, B.L. Chaperoning Roles of Macromolecules Interacting with Proteins in Vivo. Int. J. Mol. Sci. 2011, 12, 1979-1990.

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