A conserved hydrogen-bond network stabilizes the structure of Beta class glutathione S-transferases

Biochemical and Biophysical Research Communications

Volumn 382, Issue 3, 2009, Pages 525-529

  Federici, Luca ^a   Masulli, Michele ^a   Gianni, Stefano ^b   Di Ilio, Carmine ^a   Allocati, Nerino ^a  

^a UNIVERSITY OF CHIETI   (Italy)

^b CNR   (Italy)

Author keywords

Bacterial glutathione S transferase; Circular dichroism; Hydrogen bond network; Ochrobactrum anthropi; Protein stabilization

Indexed keywords

ALANINE; GLUTAMIC ACID; GLUTAREDOXIN; GLUTATHIONE TRANSFERASE; HISTIDINE; SERINE;

ALKALINITY; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DENATURATION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; OCHROBACTRUM ANTHROPI; PRIORITY JOURNAL;

ALANINE; AMINO ACID SUBSTITUTION; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GLUTAMIC ACID; GLUTATHIONE TRANSFERASE; HISTIDINE; HYDROGEN BONDING; OCHROBACTRUM ANTHROPI;

BACTERIA (MICROORGANISMS); OCHROBACTRUM ANTHROPI;

EID: 64049098665     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.052     Document Type: Article

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