STRUCTURE &FUNCTION OF HELICASES

Brookhaven Science Assoc-Brookhaven Lab, Upton NY

Investigators

Linked publications & trials

Abstract

The E coli DnaB helicase, appears to be a hexamer and requm ATP, like most helicases. A mutant had been created with a cysteine in the putative ATP-binding site in the hopes of Au-labeling the ATP-hydrolysis site in the complex. However, early Au-labeling tries seemed to make the helicase fall apart into monomers. Montse visited the lab for three months to work on Au-labeling of the helicase. One promi ig approach 1 s* to make a covalent conjugate of Au-ATP. One could use either the undecagold, which has a smaller Au core, or the Nanogold, which is more visible. One could also label ATP, ADP, or non hydrolyzable derivatives. This work is stiff in progress.