Backbone assignment of the little finger domain of a Y-family DNA polymerase

Author: Ma Dejian  

Publisher: Springer Publishing Company

ISSN: 1874-2718

Source: Biomolecular NMR Assignments, Vol.5, Iss.2, 2011-10, pp. : 195-198

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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.

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