An "Onion‐like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Issue 1 (13th October 2021)

• Record Type: Journal Article
• Authors: Politou, Anastasia S.; Pastore, Annalisa; Temussi, Piero Andrea
• Is Part Of: Chemphyschem. Volume 23:Issue 1(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-10-13
• Subjects: fluorescence -- NMR -- protein stability -- thermodynamics -- thermal unfolding; Chemistry, Physical and theoretical -- Periodicals; 541.05
• DOI: 10.1002/cphc.202100520
• Languages: English
• ISSNs: 1439-4235

Abstract

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. Abstract : Hidden complexity : Mapping of unfolding on all parts of the protein architecture by 2D NMR yields novel information on the unfolding mechanisms.