Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under nondenaturing conditions: Role of the C-terminal α-helix of the protein in folding and stability

Biochemistry

Volumn 46, Issue 12, 2007, Pages 3664-3672

  Iimura, Satoshi ^a   Umezaki, Taro ^a   Takeuchi, Makoto ^b   Mizuguchi, Mineyuki ^b   Yagi, Hiromasa ^c   Ogasahara, Kyoko ^c   Akutsu, Hideo ^c   Noda, Yasuo ^a   Segawa, Shin Ichi ^a   Yutani, Katsuhide ^d  

^a KWANSEI GAKUIN UNIVERSITY   (Japan)

^b UNIVERSITY OF TOYAMA   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; DEUTERIUM; HYDROPHOBICITY; PHYSIOLOGY; PROTEIN FOLDING; PROTONS;

HYDROPHOBIC CLUSTER; REFOLDING RATE;

ENZYME KINETICS;

5 OXOPROLYL PEPTIDASE; CYSTEINE; DEUTERIUM; MUTANT PROTEIN; SERINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION (PARAMETERS); HEAT TREATMENT; HYDROPHOBICITY; HYPERTHERMOPHILE; ION EXCHANGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SUBSTITUTION; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; POINT MUTATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PYROCOCCUS FURIOSUS; PYROGLUTAMYL-PEPTIDASE I; TEMPERATURE;

PYROCOCCUS FURIOSUS;

EID: 33947617797     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602456y     Document Type: Article

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