Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Mapping a single-molecule folding process onto a topological space


Satarifard,  Vahid
Andrea Grafmüller, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

(Publisher version), 4MB

Supplementary Material (public)
There is no public supplementary material available

Heidari, M., Satarifard, V., & Mashagh, A. (2019). Mapping a single-molecule folding process onto a topological space. Physical Chemistry Chemical Physics, 21(36), 20338-20345. doi:10.1039/C9CP03175H.

Cite as: https://hdl.handle.net/21.11116/0000-0004-8A98-5
Physics of protein folding has been dominated by conceptual frameworks including nucleation-propagation mechanism and the diffusion-collision model, none address topological properties of a chain during a folding process. Single-molecule interrogation of folded biomolecules has enabled real-time monitoring of the folding processes at an unprecedented resolution. Despite these advances, the topology landscape has not been fully mapped for any chain. Using a novel circuit topology approach, we map the topology landscape of a model polymeric chain. Inspired by single-molecule mechanical interrogation studies, we restrained the ends of a chain and followed fold nucleation dynamics. We find that, before the nucleation, transient local entropic loops dominate. Although the nucleation length of globules is dependent on the cohesive interaction, the ultimate topological states of the collapsed polymer are largely independent of the interaction but depend on the speed of the folding process. After the nucleation, transient topological rearrangements are observed that converge to a steady-state, where the fold grows in a self-similar manner.