Unfolded conformations of α-lytic protease are more stable than its native state

Nature

Volumn 395, Issue 6704, 1998, Pages 817-819

  Sohl, Julie L ^a,b   Jaswal, Sheila S ^a   Agard, David A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LYTIC PROTEINASE; PROTEINASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING KINETICS; CONCENTRATION RESPONSE; ENTROPY; ENZYME CONFORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY;

ENZYME STABILITY; EVOLUTION, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SERINE ENDOPEPTIDASES; THERMODYNAMICS;

BACTERIA (MICROORGANISMS);

EID: 0032558779     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/27470     Document Type: Article

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