Abstract:
:Sulfolobus solfataricus DNA polymerase IV (Dpo4), a prototype Y-family DNA polymerase, contains a unique little finger domain besides a catalytic core. Here, we report the chemical shift assignments for the backbone nitrogens, α and β carbons, and amide protons of the little finger domain of Dpo4. This work and our published backbone assignment for the catalytic core provide the basis for investigating the conformational dynamics of Dpo4 during catalysis using solution NMR spectroscopy.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Ma D,Fowler JD,Suo Zdoi
10.1007/s12104-011-9298-1subject
Has Abstractpub_date
2011-10-01 00:00:00pages
195-8issue
2eissn
1874-2718issn
1874-270Xjournal_volume
5pub_type
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