BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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Entry ID Data summary Entry Title Citation Title Authors
10116 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. Download bibtex for citation iamge Katsuhide Yutani, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda
10117 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. Download bibtex for citation iamge Katsuhide Yutani, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda
10052 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 Download bibtex for citation iamge Hideo Akutsu, Hiromasa Yagi, Katsuhide Yutani, Kyoko Ogasahara, Makoto Takeuchi, Mineyuki Mizuguchi, Satoshi Iimura, Shin-ichi Segawa, Taro Umezaki, Yasuo Noda