Figure 4.
 The GDDG mutation does not change the fold of the KH domain. Superimposition of 1 H– 15 N correlation spectra of wild-type (cyan) and mutant (orange) for the KH1, KH2, KH3, KH4 domains of KSRP and KH34 di-domain of ZBP1 proteins. The limited changes we observe confirm that the domains maintain their folded state.

The GDDG mutation does not change the fold of the KH domain. Superimposition of 1 H– 15 N correlation spectra of wild-type (cyan) and mutant (orange) for the KH1, KH2, KH3, KH4 domains of KSRP and KH34 di-domain of ZBP1 proteins. The limited changes we observe confirm that the domains maintain their folded state.

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