Multimer formation as a consequence of separate homodimerization domains: the human c-Jun leucine zipper is a transplantable dimerization module

The eighth sentences shpuld read as follows. rFosLZ–GST weakly associates beyond a dimer (Ka –4×104 M–1) and rJunLZ–GST associates indefinitely (Ka –4×105 M–1), consistent with an isodesmic model of association.

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Bibliographic Details
Published in:Protein engineering, design and selection design and selection, 1996-09, Vol.9 (9), p.831-831
Main Authors: Riley, L.G., Ralston, G.B., Weiss, A.S.
Format: Article
Language:English
Online Access:Get full text
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Summary:The eighth sentences shpuld read as follows. rFosLZ–GST weakly associates beyond a dimer (Ka –4×104 M–1) and rJunLZ–GST associates indefinitely (Ka –4×105 M–1), consistent with an isodesmic model of association.
ISSN:1741-0126
1741-0134
DOI:10.1093/protein/9.9.831