Thermodynamics and Solvent Effects on Substrate and Cofactor Binding inEscherichia coliChromosomal Dihydrofolate Reductase

Biochemistry ◽  
2011 ◽  
Vol 50 (18) ◽  
pp. 3673-3685 ◽  
Author(s):  
Jordan Grubbs ◽  
Sharghi Rahmanian ◽  
Alexa DeLuca ◽  
Chetan Padmashali ◽  
Michael Jackson ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Solvent Effects ◽  
Cofactor Binding

scholarly journals Diagnostic chemical shift markers for loop conformation and substrate and cofactor binding in dihydrofolate reductase complexes

2009 ◽  
Vol 12 (10) ◽  
pp. 2230-2238 ◽  
Author(s):  
Michael J. Osborne ◽  
Rani P. Venkitakrishnan ◽  
H. Jane Dyson ◽  
Peter E. Wright
Keyword(s):  
Chemical Shift ◽  
Dihydrofolate Reductase ◽  
Cofactor Binding ◽  
Loop Conformation

High-resolution gold labeling

1993 ◽  
Vol 51 ◽  
pp. 330-331
Author(s):  
James F. Hainfeld ◽  
Frederic R. Furuya ◽  
Kyra Carbone ◽  
Martha Simon ◽  
Beth Lin ◽  
...  
Keyword(s):  
Dihydrofolate Reductase ◽  
Polypeptide Chain ◽  
External Surface ◽  
Gold Cluster ◽  
Macromolecular Complex ◽  
Gold Compound ◽  
Central Cavity ◽  
Chain Folding ◽  
E Coli ◽  
Chaperonin Groel

A recently developed 1.4 nm gold cluster has been found to be useful in labeling macromolecular sites to 1-3 nm resolution. The gold compound is organically derivatized to contain a monofunctional arm for covalent linking to biomolecules. This may be used to mark a specific site on a structure, or to first label a component and then reassemble a multicomponent macromolecular complex. Two examples are given here: the chaperonin groEL and ribosomes.Chaperonins are essential oligomeric complexes that mediate nascent polypeptide chain folding to produce active proteins. The E. coli chaperonin, groEL, has two stacked rings with a central hole ∽6 nm in diameter. The protein dihydrofolate reductase (DHFR) is a small protein that has been used in chain folding experiments, and serves as a model substrate for groEL. By labeling the DHFR with gold, its position with respect to the groEL complex can be followed. In particular, it was sought to determine if DHFR refolds on the external surface of the groEL complex, or whether it interacts in the central cavity.

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