A social distancing measure governing the whole proteome

Seong Il Choi, Baik L. Seong

Research output: Contribution to journalReview articlepeer-review

Abstract

Protein folding in vivo has been largely understood in the context of molecular chaperones preventing aggregation of nascent polypeptides in the crowded cellular environment. Nascent chains utilize the crowded environment in favor of productive folding by direct physical connection with cellular macromolecules. The intermolecular repulsive forces by large excluded volume and surface charges of interacting cellular macromolecules, exerting ‘social distancing’ measure among folding intermediates, could play an important role in stabilizing their physically connected polypeptides against aggregation regardless of the physical connection types. The generic intrinsic chaperone activity of cellular macromolecules likely provides a robust cellular environment for the productive protein folding and solubility maintenance at the whole proteome level.

Original languageEnglish
Pages (from-to)104-111
Number of pages8
JournalCurrent Opinion in Structural Biology
Volume66
DOIs
Publication statusPublished - 2021 Feb

Bibliographical note

Funding Information:
This study was supported by a grant from the Ministry of Health and Welfare ( HI20C0144 ) of the Korean Government.

Publisher Copyright:
© 2020

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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