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.
Klaavuniemi et al. BMC Cell Biology 2009 10:22 doi:10.1186/1471-2121-10-22