Chemically induced self-assembly of enzyme nanorings.

Brian R. White, Qing Li, Carston R Wagner

Research output: Contribution to journalArticle

Abstract

Continued exploration into the field of chemically induced dimerization (CID) has revealed a number of applications for its use in a broader context as a method of structural assembly (1-4). In particular, the use of CID technology to generate self-assembled (and selectively disassembled) protein toroids serves as a key advancement toward developing stable and controllable protein-based platforms. Such structures have broad application to the development of novel therapeutics, lab-on-a-chip technologies, and multi-enzyme assemblies (5, 6). This chapter describes a method of developing an enzymatically active protein nanostructure incorporating both a CID-based assembly region containing dihydrofolate reductase (DHFR) and an enzymatic region consisting of histidine triad nucleotide binding protein 1 (Hint1). Details of both the production and the characterization of this structure are provided.

Original languageEnglish (US)
Pages (from-to)17-26
Number of pages10
JournalMethods in molecular biology (Clifton, N.J.)
Volume743
DOIs
StatePublished - Sep 15 2011

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Dimerization
Enzymes
Technology
Tetrahydrofolate Dehydrogenase
Proteins
Nanostructures
Histidine
Carrier Proteins
Nucleotides
Therapeutics

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Chemically induced self-assembly of enzyme nanorings. / White, Brian R.; Li, Qing; Wagner, Carston R.

In: Methods in molecular biology (Clifton, N.J.), Vol. 743, 15.09.2011, p. 17-26.

Research output: Contribution to journalArticle

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