Unfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable α-lytic protease

PLoS Computational Biology

Volumn 6, Issue 2, 2010, Pages

  Salimi, Neema L ^a   Ho, Bosco ^a   Agard, David A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; INTERFACE STATES; KINETICS; MOLECULAR DYNAMICS; THERMODYNAMICS;

COOPERATIVITY; DOMAIN INTERFACES; HIGHEST TEMPERATURE; PARTIAL UNFOLDING; PROKARYOTICS; SERINE PROTEASE; THERMODYNAMICALLY STABLE; UNFOLDED PROTEINS; UNFOLDING KINETICS; UNFOLDINGS;

PROTEINS;

ALPHA LYTIC PROTEINASE; SERINE PROTEINASE; TRYPSIN; UNCLASSIFIED DRUG; MYXOBACTER ALPHA LYTIC PROTEINASE; MYXOBACTER ALPHA-LYTIC PROTEINASE;

ARTICLE; CONTROLLED STUDY; HIGH TEMPERATURE; MOLECULAR DYNAMICS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; SIMULATION; THERMODYNAMICS; BIOLOGY; CHEMISTRY; CLUSTER ANALYSIS; METABOLISM; METHODOLOGY; PRINCIPAL COMPONENT ANALYSIS; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

PROKARYOTA;

CLUSTER ANALYSIS; COMPUTATIONAL BIOLOGY; MOLECULAR DYNAMICS SIMULATION; PRINCIPAL COMPONENT ANALYSIS; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; SERINE ENDOPEPTIDASES; TEMPERATURE; TRYPSIN;

EID: 77649223552     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000689     Document Type: Article

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