Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in ?-sheet folding.
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ABSTRACT:
SUBMITTER: Culik RM
PROVIDER: S-EPMC3354031 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Publications
Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.
Culik Robert M RM Jo Hyunil H DeGrado William F WF Gai Feng F
Journal of the American Chemical Society 20120502 19
Thioamides are sterically almost identical to their oxoamide counterparts, but they are weaker hydrogen bond acceptors. Therefore, thioamide amino acids are excellent candidates for perturbing the energetics of backbone-backbone H-bonds in proteins and hence should be useful in elucidating protein folding mechanisms in a site-specific manner. Herein, we validate this approach by applying it to probe the dynamic role of interstrand H-bond formation in the folding kinetics of a well-studied β-hair ...[more]
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