An “Onion-like” Model of Protein Unfolding: Collective versus Site Specific Approaches

Anastasia S. Politou*, Annalisa Pastore, Piero Andrea Temussi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Approximating protein unfolding by an all-or-none cooperative event is a convenient assumption that can provide precious global information on protein stability. It is however quickly emerging that the scenario is far more complex and that global denaturation curves often hide a rich heterogeneity of states that are largely probe dependent. In this review, we revisit the importance of gaining site-specific information on the unfolding process. We focus on nuclear magnetic resonance, as this is the main technique able to provide site-specific information. We review historical and most modern approaches that have allowed an appreciable advancement of the field of protein folding. We also demonstrate how unfolding is a reporter dependent event, suggesting the outmost importance of selecting the reporter carefully.

Original languageEnglish
Article numbere202100520
JournalChemPhysChem
Volume23
Issue number1
Early online date13 Oct 2021
DOIs
Publication statusPublished - 5 Jan 2022

Keywords

  • fluorescence
  • NMR
  • protein stability
  • thermal unfolding
  • thermodynamics

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