| Abstract
| - We report the first thermodynamic analysis of parallel β-sheet formation in a model system that folds in aqueous solution. NMR chemical shifts were used to determine β-sheet population, and van't Hoff anaysis provided thermodynamic parameters. Our approach relies upon the d-prolyl-1,1-dimethyl-1,2-diaminoethane unit to promote parallel β-sheet formation between attached peptide strands. The development of a macrocyclic reference molecule to provide chemical shift data for the fully folded state was crucial to the quantitative anaylsis.
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