Membrane Protein Structure Determination by Electron Cryo‐Microscopy

Tate, Christopher G.; Rubinstein, John L.

doi:10.1002/9783527621224.ch2

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Structural Investigations Of Membrane Proteins1

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2009

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“…The high-resolution three-dimensional structure of membrane proteins can be elucidated by means of NMR spectroscopy [34], X-ray crystallography [35], cryo-electron microscopy [36], or atomic force microscopy (AFM) [37]. Although nearly one third of all open reading frames in fully sequenced genomes are predicted to encode membrane proteins [1,2], it is extremely difficult to obtain high-resolution three-dimensional structures of membrane proteins.…”

Section: Structural Investigations Of Membrane Proteinsmentioning

confidence: 99%

Making the Most of Fusion Tags Technology in Structural Characterization of Membrane Proteins

2009

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Membrane proteins can be investigated at various structural levels, including the topological structure, the high-resolution three-dimensional structure, and the organization and assembly of membrane protein complexes. Gene fusion technology makes it possible to insert a polynucleotide encoding a protein or polypeptide tag into the gene encoding a membrane protein of interest. Resultant recombinant proteins may possess the functions of the original membrane proteins, together with the biochemical properties of the imported fusion tag, greatly enhancing functional and structural studies of membrane proteins. In this article, the latest literature is reviewed in relation to types, applications, strategies, and approaches to fusion tag technology for structural investigations of membrane proteins.

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