| Entry ID | 
            Original Release date | 
            Data summary | 
            Entry Title | 
            Citation Title | 
            Authors | 
                    
    
    
        | 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 |         
    
    
        | 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 |         
    
    
        | 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 |         
    
    
        | 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 |         
    
    
        | 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 |