| Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
| 50301 |
2020-07-15 |
Chemical Shifts: 1 set
|
Urea Denatured Staphylococcal Nuclease |
Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach
|
Heinrich Roder, Hisashi Okumura, Kosuke Maki, Kunio Ihara, Saho Segawa, Satoru G Itoh, Shunta Furuzawa, Takuya Mizukami, Teikichi Ikura |
| 11462 |
2013-04-04 |
Chemical Shifts: 1 set
|
One-disulfide variant of hen lysozyme: 1SS[76-94] |
Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.
|
Hideki Tachibana, Kenichi Kasai, Kuniaki Narama, Shin-Ichi Segawa, Yasuo Noda |
| 11459 |
2013-04-04 |
Chemical Shifts: 1 set
|
One-disulfide variant of hen lysozyme: 1SS[6-127] |
Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.
|
Hideki Tachibana, Kenichi Kasai, Kuniaki Narama, Shin-Ichi Segawa, Yasuo Noda |
| 11460 |
2013-04-04 |
Chemical Shifts: 1 set
|
One-disulfide variant of hen lysozyme: 1SS[30-115] |
Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.
|
Hideki Tachibana, Kenichi Kasai, Kuniaki Narama, Shin-Ichi Segawa, Yasuo Noda |
| 11461 |
2013-04-04 |
Chemical Shifts: 1 set
|
One-disulfide variant of hen lysozyme: 1SS[64-80] |
Glycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.
|
Hideki Tachibana, Kenichi Kasai, Kuniaki Narama, Shin-Ichi Segawa, Yasuo Noda |
| 11428 |
2011-09-28 |
Chemical Shifts: 1 set
|
1H, 15N chemical shift assignments for a disulfide-deficient mutant of the starch-binding domain of glucoamylase |
NMR analysis of a kinetically trapped intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase
|
Hayuki Sugimoto, Shin-ichi Segawa, Yasuo Noda |
| 11051 |
2009-04-29 |
Chemical Shifts: 1 set
|
Disulfide-free variant of hen lysozyme: 0SS |
Glycerol-induced folding of unstructured disulfide-deficient lysozyme into a native-like conformation
|
Gakuji Doi, Hideki Tachibana, Keiko Sakamoto, Ken-ichi Hirai, Kouta Yamazaki, Mitsunobu Yusa, Naoki Tokunaga, Shin-Ichi Segawa, Yasuo Noda, Yoshiaki Kitamura |
| 11052 |
2009-04-29 |
Chemical Shifts: 1 set
|
Two-disulfide variant of hen lysozyme: 2SS[6-127, 64-80] |
Glycerol-induced folding of unstructured disulfide-deficient lysozyme into a native-like conformation
|
Gakuji Doi, Hideki Tachibana, Keiko Sakamoto, Ken-ichi Hirai, Kouta Yamazaki, Mitsunobu Yusa, Naoki Tokunaga, Shin-Ichi Segawa, Yasuo Noda, Yoshiaki Kitamura |
| 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 |
| 7160 |
2008-11-12 |
Chemical Shifts: 1 set
|
1H chemical shift assignments of metLYZ at pH 3.8 and 25 C |
NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure
|
A Yokota, D Horii, H Tachibana, S Segawa, T Tominaga, Y Noda, Y Tanisaka |
| 7159 |
2008-11-12 |
Chemical Shifts: 1 set
|
1H chemical shift assignments of 2SS[6-127, 30-115] at pH 3.8 and 25 C |
NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure
|
A Yokota, D Horii, H Tachibana, S Segawa, T Tominaga, Y Noda, Y Tanisaka |
| 7135 |
2008-11-12 |
Chemical Shifts: 1 set
|
Assignments of 2SSalpha in 8M urea, pH 2, 293 K |
Characterisation of Disulfide Bond Dynamics in Non-Native States of Lysozyme and its Disulfide Deletion Mutants by NMR
|
Christopher M Dobson, Emily S Collins, Harald Schwalbe, Hideki Tachibana, Julia Wirmer, Kenichi Hirai, Shin-ichi Segawa |
| 7136 |
2008-11-12 |
Chemical Shifts: 1 set
|
Assignments of 2SSbeta in 8M urea, pH 2, 293 K |
Characterisation of Disulfide Bond Dynamics in Non-Native States of Lysozyme and its Disulfide Deletion Mutants by NMR
|
Christopher M Dobson, Emily S Collins, Harald Schwalbe, Hideki Tachibana, Julia Wirmer, Kenichi Hirai, Shin-ichi Segawa |
| 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 |
| 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 |
| 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 |
| 5069 |
2003-05-22 |
Chemical Shifts: 1 set
|
NMR Structural Study of Two-Disulfide Variant of hen Lysozyme: 2SS[6-127, 30-115]-A Disulfide Intermediate with a Partly Unfolded Structure |
NMR Structural Study of Two-disulfide Variant of hen Lysozyme : 2SS[6-127, 30-115]--A Disulfide Intermediate with a Partly Unfolded Structure
|
Atsushi Yokota, Daisuke Horii, Hideki Tachibana, Shin-ichi Segawa, Takeshi Tominaga, Yasuo Noda, Yoshiaki Tanisaka |
| 5068 |
2003-12-22 |
Chemical Shifts: 1 set
|
Recombinant hen lysozyme containing the extra N-terminal Met as the standard reference for the study of hen lysozyme variants |
NMR Structural Study of Two-disulfide Variant of hen Lysozyme: 2SS[6-127, 30-115]--A Disulfide Intermediate with a Partly Unfolded Structure
|
Atsushi Yokota, Daisuke Horii, Hideki Tachibana, Shin-ichi Segawa, Takeshi Tominaga, Yasuo Noda, Yoshiaki Tanisaka |
