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. Author manuscript; available in PMC: 2009 Oct 14.
Published in final edited form as: Biochemistry. 2008 Sep 20;47(41):10933–10939. doi: 10.1021/bi8008278

Figure 3.

Figure 3

Overlay of the NMR HSQC spectra of TMEGF45 wild type with the mutant Y358A. The wild type spectrum is in blue, and the mutant spectrum is in red. Samples were 0.25 mM with a final volume of 0.45 mL in 90% H2O/10% 2H2O with 2 mM NaN3, pH 6.5. 1H-15N HSQC were collected at 310 K on a Bruker DRX600 (wild type) or a Bruker DMX500 (Y358A). Many of the cross peaks that are missing from the spectrum of the Y358A mutant can be assigned to the fourth EGF-like domain suggesting that mutation of Tyr 358 to Ala results in a defect in folding of this domain. Some of the fourth domain peaks are labeled, and some fifth domain peaks that are observed in both spectra are labeled with boxes.