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Analysis of the solution conformations of T4 lysozyme by paramagnetic NMR spectroscopy

Chen, Jia-Liang; Yang, Yin; Zhang, Lin-Lin; Liang, Haobo; Huber, Thomas; Su, Xun-Cheng; Otting, Gottfried

Description

A large number of crystal structures of bacteriophage T4 lysozyme (T4-L) have shown that it contains two subdomains, which can arrange in a compact conformation (closed state) or, in mutants of T4-L, more extended structures (open state). In solution, wild-type T4-L displays only a single set of nuclear magnetic resonance (NMR) signals, masking any conformational heterogeneity. To probe the conformational space of T4-L, we generated a site-specific lanthanide binding site by attaching...[Show more]

CollectionsANU Research Publications
Date published: 2016-02-17
Type: Journal article
URI: http://hdl.handle.net/1885/148501
Source: Physical chemistry chemical physics : PCCP
DOI: 10.1039/c5cp07196h

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