A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein

Biochemistry

Volumn 39, Issue 14, 2000, Pages 4182-4190

  Konno, Takashi ^a   Kamatari, Yuji O ^b   Tanaka, Naoki ^c   Kamikubo, Hironari ^d   Dobson, Christopher M ^b   Nagayama, Kuniaki ^a  

^a NATIONAL INSTITUTE FOR PHYSIOLOGICAL SCIENCES   (Japan)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

^d INSTITUTE OF MATERIALS STRUCTURE SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME PRECURSOR; PEPSIN A;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEMENT ACTIVATION; CONFORMATIONAL TRANSITION; DATA ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RADIATION SCATTERING;

ALKYLATING AGENTS; ANIMALS; ENZYME PRECURSORS; ENZYME STABILITY; PEPSIN A; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0034636112     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991923d     Document Type: Article

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