NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A - A marginally stable state in folded proteins

Biochemistry

Volumn 43, Issue 21, 2004, Pages 6663-6669

  Yokota, Atsushi ^a   Hirai, Kenichi ^b   Miyauchi, Hiroyo ^b   Iimura, Satoshi ^b   Noda, Yasuo ^b   Inoue, Kyoko ^c   Akasaka, Kazuyuki ^d   Tachibana, Hideki ^e   Segawa, Shin Ichi ^b  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b KWANSEI GAKUIN UNIVERSITY   (Japan)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

^d KINKI UNIVERSITY   (Japan)

^e KOBE UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ENZYME KINETICS; HYDROGEN BONDS; HYDROPHOBICITY; NITROGEN COMPOUNDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

AMIDE HYDROGEN EXCHANGE RATES; LYSOZYMES;

BIOCHEMISTRY;

AMIDE; ENZYME VARIANT; LYSOZYME;

ARTICLE; BETA SHEET; DISULFIDE BOND; HEN; HYDROGEN BOND; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; WILD TYPE;

AMIDES; DISULFIDES; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MURAMIDASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 2542589513     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049967w     Document Type: Article

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