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(a)
9.0
8.5
8.0
7.5
F2 (ppm)
7.0
6.5
(b)
9.0
8.5
8.0
7.5
F2 (ppm)
7.0
6.5
Figure 5.19 Portions of NOESY spectra of kinaseX inhibitor 1 in complex with residue type
specifically protonated samples of kinaseX. Intra-ligand cross peaks are circled in both spectra.
(A) KinaseX inhibitor 1 in complex with [ 1 H ]Leu (otherwise 2 H -labeled) kinaseX. Concentra-
tions of both the protein and the inhibitor used were 140 μM. (B) KinaseX inhibitor 1 in complex
with [ 1 H ]Val (otherwise 2 H -labeled) kinaseX. Concentrations of both the protein and the inhib-
itor were 90 μM. Both spectra (A) and (B) were recorded at 15 °C, 600 MHz 1 H frequency,
using a NOESY mixing time of 60 ms.
NOEs). Failure to do so can result in the generation of highly inaccurate structures. Regard-
less of the labeling scheme, one must take care to choose a mixing time, or range of mixing
times, that yields an adequate number of NOEs without suffering from severe spin diffu-
sion effects. Although we are still gaining experience with the number of NOEs required
to ensure reliable pose identification, for the systems that we have studied to date we have
had from 9 to 22 NOEs per ligand proton group.
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