Enthalpically driven peptide stabilization by protective osmolytes

2010/01/01 by Regina Politi, Daniel Harries · 3 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Lipid Membrane Structure and Behavior #Protein Structure and Dynamics #Mass Spectrometry Techniques and Applications

paper · doi:10.1039/c0cc01763a

openalex publication_date 2010/01/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/05

Abstract

We determined the added enthalpic and entropic contributions of protective osmolytes to the folding of a model peptide into its native beta-hairpin state. In contrast to entropically driven steric "crowding", this study shows that sugars and polyols can act as protective osmolytes by primarily diminishing the unfavourable enthalpic contribution to folding.

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