A single disulfide bond restores thermodynamic and proteolytic stability to an extensively mutated protein

Protein Science

Volumn 9, Issue 9, 2000, Pages 1642-1650

  Roesler, Keith R ^a   Rao, A Gururaj ^a  

^a PIONEER HI BRED INTERNATIONAL INC   (United States)

Author keywords

Barley chymotrypsin inhibitor 2; Essential amino acids; Protein conformation; Protein engineering; Protein stability; Thermodynamic stability

Indexed keywords

CHYMOTRYPSIN INHIBITOR; MUTANT PROTEIN;

AMINO ACID COMPOSITION; AMINO ACID SUBSTITUTION; ARTICLE; BARLEY; DISULFIDE BOND; NONHUMAN; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMODYNAMICS;

HORDEUM VULGARE SUBSP. VULGARE;

EID: 0033810120     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.9.1642     Document Type: Article

References (42)

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15. Role of arginine 67 in the stabilization of chymotrypsin Inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein
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