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Capturing conformational states in proteins using sparse paramagnetic NMR data

Pilla, Kala Bharath; Leman, Julia Koehler; Huber, Thomas; Otting, Gottfried

Description

Capturing conformational changes in proteins or protein-protein complexes is a challenge for both experimentalists and computational biologists. Solution nuclear magnetic resonance (NMR) is unique in that it permits structural studies of proteins under greatly varying conditions, and thus allows us to monitor induced structural changes. Paramagnetic effects are increasingly used to study protein structures as they give ready access to rich structural information of orientation and long-range...[Show more]

CollectionsANU Research Publications
Date published: 2015-05-18
Type: Journal article
URI: http://hdl.handle.net/1885/16071
Source: PLOS ONE
DOI: 10.1371/journal.pone.0127053

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