Single molecule force spectroscopy reveals the context dependent folding pathway of the C-terminal fragment of Top7.

ABSTRACT: Top7 is a de novo designed protein with atomic level accuracy and shows a folded structure not found in nature. Previous studies showed that the folding of Top7 is not cooperative and involves various folding intermediate states. In addition, various fragments of Top7 were found to fold on their own in isolation. These features displayed by Top7 are distinct from those of naturally occurring proteins of a similar size and suggest a rough folding energy landscape. However, it remains unknown if and how the intra-polypeptide chain interactions among the neighboring sequences of Top7 affect the folding of these Top7 fragments. Here we used single-molecule optical tweezers to investigate the folding-unfolding pathways of full length Top7 as well as its C-terminal fragment (CFr) in diffe

SUBMITTER: Li J 

PROVIDER: S-EPMC8179357 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature