Figure 5

Structural analysis of ALP107-273. A) The CD spectrum of ALP107-273 is consistent with a random coil conformation, whereas the PDZ domain containing ALP1-273 fragment has some β-strand features. B) Overlaid ¹⁵N HSQC NMR spectra of 1.6 mM ALP107-273 in the purification buffer (green) and after addition of 40 mM Asp (red). C) ¹⁵N-HSQC spectrum of 84 μM ALP107-273 in the presence of 218 μM unlabelled R1-R4. D) Identical spectra as in C taken from 80 μM μM ALP107-273 alone. The low intensity signals in the lower right part of the spectra in C and D are observed for ALP concentrations under 100 μM, and apparently represent another conformation of ALP. Owing to low sample concentration, no attempt was made to assign these signals.