Protein folding: An antagonistic reaction of spontaneous folding and diffusion limited aggregation in nature

Chia-Ching Chang*, Lou Sing Kan

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Protein folding may follow a spontaneous process or a reaction-path directed process, determined by various folding transition boundaries due to intrinsic properties of the protein. A general first-order-like state-transition model predicts that a protein might be trapped in an aggregated state when the folding path crosses the transition boundary. Both experimental study and molecular simulation indicated that protein within this particular transition region might involve intermolecular interactions. Therefore, a direct folding process may have been a combination of an antagonistic reaction of spontaneous folding and a diffusion limited aggregation. In this paper, the protein folding mechanism and the theoretical basis of time limited diffusion/aggregation process are elaborated. The application of auto-correlation function in time dependent biological studies is also discussed.

Original languageEnglish
Pages (from-to)693-702
Number of pages10
JournalChinese Journal of Physics
Volume45
Issue number6 II
StatePublished - 1 Dec 2007

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