Gaku Aoki   Toyo K. Yamada   Mayu Arii   Shuichi Kojima   Tadashi Mizoguchi   
JOURNAL OF BIOCHEMISTRY 144(1) 15-19 2008年7月
One feature of the alpha 3-peptide, which has the amino acid sequence of (Leu-Glu-Thr-Leu-Ala-Lys-Ala)(3), that distinguishes it from many other alpha-helix-forming peptides is its ability to form fibrous assemblies that can be observed by transmi...
Shuichi Kojima   Akane Iwahara   Yuri Hisano   Hideyuki Yanai   
PROTEIN ENGINEERING DESIGN & SELECTION 20(5) 211-217 2007年5月
We previously demonstrated that Pleurotus ostreatus proteinase A inhibitor I (POIA1) could function as an intramolecular chaperone of subtilisin BPN', as in the case of the propeptide of subtilisin BPN', and that its Phe44 -> Ala mutant, which ...
Shuichi Kojima   Akane Iwahara   Yuri Hisano   Hideyuki Yanai   
PROTEIN ENGINEERING DESIGN & SELECTION 20(5) 211-217 2007年5月
We previously demonstrated that Pleurotus ostreatus proteinase A inhibitor I (POIA1) could function as an intramolecular chaperone of subtilisin BPN', as in the case of the propeptide of subtilisin BPN', and that its Phe44 -> Ala mutant, which ...
T Takei   A Okonogi   K Tateno   A Kimura   S Kojima   K Yazaki   K Miura   
JOURNAL OF BIOCHEMISTRY 139(2) 271-278 2006年2月
The polypeptide alpha 3, which was synthesized by us to produce an amphipathic helix structure, contains the regular three times repeated sequence (LETLAKA)(3), and alpha 3 forms a fibrous assembly. To clarify how the side chains of amino acid res...