| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 10116 |
2008-06-27 |
Chemical Shifts: 1 set
|
The Confirmation of the Denatured Structure of Pyrrolidone Carboxyl Peptidase under Non denaturing Conditions: Helix Propensity of wild-type H6-peptide |
The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution.
|
Katsuhide Yutani, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda |
| 10117 |
2008-06-27 |
Chemical Shifts: 1 set
|
The Confirmation of the Denatured Structure of Pyrrolidone carboxyl Peptidase under Non denaturing Conditions: Deference in Helix Propensity of Two Synthetic Peptides with Single Amino Acid Substitution |
The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution.
|
Katsuhide Yutani, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda |
| 10052 |
2007-06-13 |
Chemical Shifts: 2 sets
|
characterization of PCP-0SH in the D1 state was examined by using H/D exchange experiments. |
Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under non-denaturing conditions: Role of the C-terminal a-helix of the protein in folding and stability
|
Hideo Akutsu, Hiromasa Yagi, Katsuhide Yutani, Kyoko Ogasahara, Makoto Takeuchi, Mineyuki Mizuguchi, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda |
| 6415 |
2005-04-04 |
Chemical Shifts: 1 set
|
Three-disulfide variant of hen lysozyme: C30A/C115A |
NMR Characterization of Three-Disulfide Variants of Lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A -A Marginally Stable State in Folded Proteins
|
Atsushi Yokota, Hideki Tachibana, Hiroyo Miyauchi, Kazuyuki Akasaka, Kenichi Hirai, Kyouko Inoue, Satoshi Iimura, Shin-ichi Segawa, Yasuo Noda |
| 5803 |
2004-09-14 |
Chemical Shifts: 1 set
|
Three-disulfide variant of hen lysozyme: C64A/C80A |
NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.
|
Atsushi Yokota, Hideki Tachibana, Hiroyo Miyauchi, Kazuyuki Akasaka, Kenichi Hirai, Kyouko Inoue, Satoshi Iimura, Shin-ichi Segawa, Yasuo Noda |
| 5804 |
2004-09-14 |
Chemical Shifts: 1 set
|
Three-disulfide variant of hen lysozyme: C76A/C94A |
NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.
|
Atsushi Yokota, Hideki Tachibana, Hiroyo Miyauchi, Kazuyuki Akasaka, Kenichi Hirai, Kyouko Inoue, Satoshi Iimura, Shin-ichi Segawa, Yasuo Noda |
