학술논문
I. Association behavior of ACHC-rich beta-peptide foldamers. II. Fluorine-19 NMR methods for monitoring alpha-peptide folding .
Document Type
Theses
Author
Source
Dissertation Abstracts International; Dissertation Abstract International; 70-03B.
Subject
Language
English
Abstract
Summary: 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.