The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability

Protein Science

Volumn 13, Issue 2, 2004, Pages 381-390

  Truhlar, Stephanie M E ^a   Cunningham, Erin L ^a   Agard, David A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Kinetic stability; Pro region; Protein evolution; Protein folding; Streptomyces griseus protease B

Indexed keywords

PROTEINASE; PROTEINASE B; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENERGY TRANSFER; ENZYME CONFORMATION; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; STREPTOMYCES GRISEUS; THERMODYNAMICS;

AMINO ACID SEQUENCE; ENZYME STABILITY; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN DENATURATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; STREPTOMYCES GRISEUS; THERMODYNAMICS; TRYPSIN;

BACTERIA (MICROORGANISMS); MAMMALIA; STREPTOMYCES GRISEUS;

EID: 1642493928     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03336804     Document Type: Article

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