Extracellular domain of mouse Notch-1 EGF12

Digital lock system by Bruker instrument was used to set chemical shift reference. DHO signal showed 4.704 ppm at 300K.

Journal of the American Chemical Society
Chemical synthesis, folding, and structural insights into O-fucosylated epidermal growth factor-like repeat 12 of mouse Notch-1 receptor.

NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1 EGF12 domain
The C terminus Isoleucine 38 id not free form from COOH but CONH2

Structure Of Sugar Modified Epidermal Growth Factor-Like Repeat 12 Of Mouse Notch-1 Receptor

Structure Of Epidermal Growth Factor-Like Repeat 12 Of Mouse Notch-1 Receptor

Structure Of O-Fucosylated Epidermal Growth Factor-Like Repeat 12 Of Mouse Notch-1 Receptor

The naked EGF12 was dissolved in solvent at pH 5.3. The pH was adjusted to 5.3 by addition of NaOH and HCl.

NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1

I used NMRPipe software for data processing then used SPARKY software to assign the chemical shift.

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax