Abstract:
:Molecular dynamics simulations are presented for a Thermus aquaticus (Taq) DNA polymerase I complex (consisting of the protein, the primer-template DNA strands, and the incoming nucleotide) subjected to external forces. The results obtained with a force applied to the DNA template strand provide insights into the effect of the tension on the activity of the enzyme. At forces below 30 pN a local model based on the parameters determined from the simulations, including the restricted motion of the DNA bases at the active site, yields a replication rate dependence on force in agreement with experiment. Simulations above 40 pN reveal large conformational changes in the enzyme-bound DNA that may have a role in the force-induced exonucleolysis observed experimentally.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Andricioaei I,Goel A,Herschbach D,Karplus Mdoi
10.1529/biophysj.103.039313subject
Has Abstractpub_date
2004-09-01 00:00:00pages
1478-97issue
3eissn
0006-3495issn
1542-0086pii
S0006-3495(04)73632-2journal_volume
87pub_type
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