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Resonance assignments of the 56 kDa chimeric avidin in the biotin-bound and free forms

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Details

Original languageEnglish
Pages (from-to)35-38
Number of pages4
JournalBIOMOLECULAR NMR ASSIGNMENTS
Volume7
Issue number1
DOIs
Publication statusPublished - Apr 2013
Publication typeA1 Journal article-refereed

Abstract

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.

ASJC Scopus subject areas

Keywords

  • Biotin, Chimeric avidin, Ligand binding, NMR, Thermostability