Sekiguchi Mitsuhiro
,
Kobashigawa Yoshihiro
,
Kawasaki Masashi
,
Yokochi Masashi
,
Kiso Tetsuo
,
Suzumura Ken-ichi
,
Mori Keitaro
,
Teramura Toshio
,
Inagaki Fuyuhiko
… The fusion protein exhibited increased solubility and stability compared with the isolated FRB domain, and facilitated the analysis of rapamycin and FK506 binding using differential scanning calorimetry (DSC) and solution nuclear magnetic resonance (NMR). … DSC enabled the rapid observation of protein-drug interactions at the domain level, while NMR gave insights into the protein-drug interactions at the residue level. …
Protein Engineering, Design and Selection 24(11), 811-817, 2011-11
IR
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