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EPR spectroscopy identifies Met and Lys residues that are essential for the interaction between the CusB N-terminal domain and metallochaperone CusF. Issue 7 (8th July 2015)
Record Type:
Journal Article
Title:
EPR spectroscopy identifies Met and Lys residues that are essential for the interaction between the CusB N-terminal domain and metallochaperone CusF. Issue 7 (8th July 2015)
Main Title:
EPR spectroscopy identifies Met and Lys residues that are essential for the interaction between the CusB N-terminal domain and metallochaperone CusF
<abstract abstract-type="toc"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <graphic position="anchor" id="ga" xlink:href="ark:/27927/pgj2687q1vg" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" />Methionine and lysine residues are important for preserving the structure of the CusB N-terminal domain and for the interaction with CusF.</p> </abstract>