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. 2009 Sep 4;10(13):2177-81.
doi: 10.1002/cbic.200900380.

In situ monitoring of backbone thioester exchange by 19F NMR

William C Pomerantz  1 , Erik B Hadley, Charles G Fry, Samuel H Gellman
Affiliations

In situ monitoring of backbone thioester exchange by 19F NMR

William C Pomerantz et al. Chembiochem. .
No abstract available

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Figures

Figure 1
Figure 1
19F and 19F{1H} NMR data. A) 19F resonances observed for NT-F and HSF when HSF is mixed with a nonfluorine-labeled peptide thioester.[15] B) 19F{1H} resonances observed for NT-Cf and HSCf when HSCf is mixed with a nonfluorine-labeled thioester.[15] C) 19F resonances observed for the BTE mixture depicted in Scheme 1B.
Figure 2
Figure 2
Correlation of Δδ(δ19F [NT-Cf] −δ19F [HSCf]) with ΔGFold previously determined by HPLC for various a-d′ combinations. The ΔGFold values were determined with a system[3] similar to that shown in Scheme 1 (see the main text for a description of the modifications necessary for HPLC measurement). Residues a1′=a2′=Leu.
Figure 3
Figure 3
Partial helical net diagram for the intramolecular coiled-coil inter-face in NT-Cf. The N-terminal segment is shown with solid lines, the C-terminal segment is shown with dashed lines and varied positions a/a1′/a2′ are indicated by dashed and filled circles.
Scheme 1
Scheme 1
A) Top: sequence of NT-Cf; Succ = N-terminal succinyl group, Z = 3,5-difluorophenylalanine. Below are the sequences of NT-F (middle) and HSCf (bottom). Residues a/a1′/d′/a2′ correspond to mutation sites. B) Thioester exchange process for NT-Cf. The thioesterthiol pair on the left comprises N-terminal segment NT-F, and C-terminal segment HSCf, while the pair on the right contains the full-length coiled-coil NT-Cf, and a small thiol HSF.
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References

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