Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms
Research output: Contribution to journal › Article › Scientific › peer-review
|Number of pages||4|
|Journal||BIOMOLECULAR NMR ASSIGNMENTS|
|Publication status||Published - Apr 2013|
|Publication type||A1 Journal article-refereed|
Avidin is a homotetrameric ~56 kDa protein found in chicken egg white. Avidin's ability to bind biotin with a very high affinity has widely been exploited in biotechnological applications. Protein engineering has further diversified avidin's feasibility. ChiAVD(I117Y) is a product of rational protein engineering. It is a hyperthermostable synthetic hybrid of avidin and avidin-related protein 4 (AVR4). In this chimeric protein a 23-residue segment in avidin has been replaced with the corresponding sequence found in AVR4, and a point mutation at subunit interface 1-3 (and 2-4) has been introduced. Here we report the backbone and sidechain resonance assignments of the biotin-bound form of ChiAVD(I117Y) as well as the backbone resonance assignments of the free form.