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Updated: Jun 23, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA
Chris A Brosey1, Marie-Eve Chagot, Mark Ehrhardt
1Department of Biochemistry, and Center for Structural Biology, Vanderbilt University, Nashville, Tennessee 37232-8725, USA.
Abstract:
Modular proteins with multiple domains tethered by flexible linkers have variable global architectures. Using the eukaryotic ssDNA binding protein, Replication Protein A (RPA), we demonstrate that NMR spectroscopy is a powerful tool to characterize the remodeling of architecture in different functional states. The first direct evidence is obtained for the remodeling of RPA upon binding ssDNA, including an alteration in the availability of the RPA32N domain that may help explain its damage-dependent phosphorylation.
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