Analysis of the solution conformations of T4 lysozyme by paramagnetic NMR spectroscopy
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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]
Collections | ANU Research Publications |
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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 |
Access Rights: | Open Access |
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File | Description | Size | Format | Image |
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PhysChemChemPhys2016_18_5850.pdf | 4.1 MB | Adobe PDF |
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