Where the complex things are: single molecule and ensemble spectroscopic investigations of protein folding dynamics. (February 2016)

• Record Type: Journal Article
• Authors: Takahashi, Satoshi; Kamagata, Kiyoto; Oikawa, Hiroyuki
• Is Part Of: Current opinion in structural biology. Volume 36(2016)
• Page Start: 1
• Page End: 9
• Publication Date: 2016-02
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2015.11.006
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: The transition path of small proteins can be explained by the native centric model. The size of the unfolded proteins in the absence of denaturants is controversial. The unfolded state of small proteins possesses substates with residual structures. Even small single domain proteins demonstrate complex folding dynamics. Large proteins are distinct and show rapid collapse with long-range contacts. Abstract : Progress in our understanding of the simple folding dynamics of small proteins and the complex dynamics of large proteins is reviewed. Recent characterizations of the folding transition path of small proteins revealed a simple dynamics explainable by the native centric model. In contrast, the accumulated data showed the substates containing residual structures in the unfolded state and partially populated intermediates, causing complexity in the early folding dynamics of small proteins. The size of the unfolded proteins in the absence of denaturants is likely expanded but still controversial. The steady progress in the observation of folding of large proteins has clarified the rapid formation of long-range contacts that seem inconsistent with the native centric model, suggesting that the folding strategy of large proteins is distinct from that of small proteins.