Single-Molecule Force Spectroscopy of Protein Folding

• Author(s) / Creator(s)

  • Petrosyan, Rafayel
  • Narayan, Abhishek
  • Woodside, Michael T

• The use of force probes to induce unfolding and refolding of single molecules through the application of mechanical tension, known as single-molecule force spectroscopy (SMFS), has proven to be a powerful tool for studying the dynamics of protein folding. Here we provide an overview of what has been learned about protein folding using SMFS, from small, single-domain proteins to large, multi-domain proteins. We highlight the ability of SMFS to measure the energy landscapes underlying folding, to map complex pathways for native and non-native folding, to probe the mechanisms of chaperones that assist with native folding, to elucidate the effects of the ribosome on co-translational folding, and to monitor the folding of membrane proteins.

• Date created

  2021-10-01

• Subjects / Keywords

  • Force spectroscopy
  • Protein folding and misfolding
  • Chaperones
  • Co-translational folding
  • Membrane protein folding

• Type of Item

  Article (Draft / Submitted)

• DOI

  https://doi.org/10.7939/r3-hq2g-4n56

• License

  Attribution-NonCommercial-NoDerivatives 4.0 International