Thermodynamic effects of active-site ligands on the reversible, partial unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric studies

Biochemistry ◽  
1992 ◽  
Vol 31 (48) ◽  
pp. 11991-12000 ◽  
Author(s):  
Michal Zolkiewski ◽  
Ann Ginsburg
Keyword(s):  
Escherichia Coli ◽  
Glutamine Synthetase ◽  
Active Site ◽  
Partial Unfolding ◽  
Thermodynamic Effects ◽  
Calorimetric Studies

Thermodynamic effects of reduction of the active-site disulfide of Escherichia coli thioredoxin explored by differential scanning calorimetry

Biochemistry ◽  
1994 ◽  
Vol 33 (12) ◽  
pp. 3688-3692 ◽  
Author(s):  
John E. Ladbury ◽  
Nand Kishore ◽  
Homme W. Hellinga ◽  
Richard Wynn ◽  
Julian M. Sturtevant
Keyword(s):  
Escherichia Coli ◽  
Differential Scanning Calorimetry ◽  
Active Site ◽  
Scanning Calorimetry ◽  
Thermodynamic Effects

Partial unfolding of dodecameric glutamine synthetase from Escherichia coli: temperature-induced, reversible transitions of two domains

Biochemistry ◽  
1989 ◽  
Vol 28 (15) ◽  
pp. 6281-6294 ◽  
Author(s):  
Andrew Shrake ◽  
Mark T. Fisher ◽  
Patrick J. McFarland ◽  
Ann Ginsburg
Keyword(s):  
Escherichia Coli ◽  
Glutamine Synthetase ◽  
Partial Unfolding ◽  
Reversible Transitions
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