Enthalpically driven peptide stabilization by protective osmolytes.
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.
Politi
Regina
R
Institute of Chemistry and The Fritz Haber Research Center, The Hebrew University, Jerusalem 91904, Israel.
Harries
Daniel
D
D002241:Carbohydrates / Q000737:chemistry; D009994:Osmolar Concentration; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D002241:Carbohydrates; D010455:Peptides; D011108:Polymers; C024617:polyol