In a separate investigation, we use 19F NMR to develop new methods for quantifying the thermodynamics of folding within a coiled-coil model system. Our method employs a technique called backbone thioester exchange (BTE). We find that the 19F NMR approach allows assessment of folded state stability for a full-length thiodepsipeptide coiled-coil even before chemical equilibrium has been achieved, if sufficient calibration data are available. Thus, BTE by 19F NMR enables rapid screening of sets of alpha-peptide variants to identify sequences that confer the greatest conformational stability.... H., aquot;Toward p-Peptide Tertiary Structure: Self-Association of an Amphiphilic 14- Helix in Aqueous Solution, aquot; Org. Lett., 2001, ... (53) Rathore, N.; de Pablo, J. J.; Gellman, S., H., aquot;Thermodynamic stability of beta-peptide helices and the role ofanbsp;...
|Title||:||I. Association Behavior of ACHC-rich Ss-peptide Foldamers|
|Author||:||William Charles Pomerantz|
|Publisher||:||ProQuest - 2008|