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Biochemical, biophysical, and proteomic approaches to study DNA helicases Vindigni AMol Biosyst 2007[Apr]; 3 (4): 266-74Helicases are a family of enzymes that play an essential role in nearly all DNA metabolic processes, catalyzing the transient opening of DNA duplexes. These motor proteins couple the chemical energy of ATP binding and hydrolysis to the separation of the complementary strands of a DNA or RNA duplex substrate. A full understanding of their mechanism of DNA unwinding can be achieved only through careful investigation of the thermodynamic and kinetic parameters that control this ATP-driven process, as well as through analysis of the helicases' tertiary and quaternary structures associated with nucleic acids and/or nucleotide recognition. This review describes the various biochemical, biophysical, and, more recently, proteomic techniques that have been developed to shed light on the still controversial, and in some aspects elusive, helicase-catalyzed mechanism of DNA unwinding.|*Proteomics[MESH]|Adenosine Triphosphate/metabolism[MESH]|DNA Helicases/*chemistry/physiology[MESH]|DNA/*chemistry/metabolism[MESH]|Hydrolysis[MESH]|Models, Genetic[MESH]|Protein Binding[MESH]|Protein Structure, Quaternary[MESH]|RNA/chemistry/metabolism[MESH]|Structure-Activity Relationship[MESH]|Substrate Specificity[MESH] |
