The ability of chemical denaturants to perturb protein structures is well-established, but the physico-chemical basis underlying this phenomenon is still debated. In the present review, we survey classical and recent literature to provide a global overview of the effects that chemical denaturants produce on the different structural states of proteins, from globular to intrinsically disordered and amyloid-like assemblies. Interestingly, the different forces that stabilize these distinct structural states generate intriguing effects. Even the ranking of the relative strength of the most common denaturants (i.e., urea and guanidinium ion), which is well-established and generally conserved for globular proteins, is not fully suited for other structural states. Analysis of available data, using both polymer physics and atomic-interaction-based perspectives, provides complementary and somehow convergent views of the mechanism of action of chemical denaturants. The different “quality” of water as a solvent in distinct contexts, and the remarkable promiscuity of chemical denaturants represent useful conceptual frameworks to shed light on these intricate phenomena.

The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins

Paladino A
Primo
;
Vitagliano L;
2023

Abstract

The ability of chemical denaturants to perturb protein structures is well-established, but the physico-chemical basis underlying this phenomenon is still debated. In the present review, we survey classical and recent literature to provide a global overview of the effects that chemical denaturants produce on the different structural states of proteins, from globular to intrinsically disordered and amyloid-like assemblies. Interestingly, the different forces that stabilize these distinct structural states generate intriguing effects. Even the ranking of the relative strength of the most common denaturants (i.e., urea and guanidinium ion), which is well-established and generally conserved for globular proteins, is not fully suited for other structural states. Analysis of available data, using both polymer physics and atomic-interaction-based perspectives, provides complementary and somehow convergent views of the mechanism of action of chemical denaturants. The different “quality” of water as a solvent in distinct contexts, and the remarkable promiscuity of chemical denaturants represent useful conceptual frameworks to shed light on these intricate phenomena.
2023
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli
denaturants, urea, guanidinium, solvent, conformational ensemble, intrinsically disordered proteins
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/494381
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