Enthalpically driven peptide stabilization by protective osmolytes

Regina Politi, Daniel Harries*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

101 Scopus citations

Abstract

We determined the added enthalpic and entropic contributions of protective osmolytes to the folding of a model peptide into its native β-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.

Original languageAmerican English
Pages (from-to)6449-6451
Number of pages3
JournalChemical Communications
Volume46
Issue number35
DOIs
StatePublished - 21 Sep 2010

Fingerprint

Dive into the research topics of 'Enthalpically driven peptide stabilization by protective osmolytes'. Together they form a unique fingerprint.

Cite this