Reference - Detail
| RRC ID | 21532 |
|---|---|
| Author | Ito Y, Mikawa T, Smith BO. |
| Title | In-cell NMR of intrinsically disordered proteins in prokaryotic cells. |
| Journal | Methods Mol Biol |
| Abstract |
In-cell NMR, i.e., the acquisition of heteronuclear multidimensional NMR of biomacromolecules inside living cells, is, to our knowledge, the only method for investigating the three-dimensional structure and dynamics of proteins at atomic detail in the intracellular environment. Since the inception of the method, intrinsically disordered proteins have been regarded as particular targets for in-cell NMR, due to their expected sensitivity to the molecular crowding in the intracellular environment. While both prokaryotic and eukaryotic cells can be used as host cells for in-cell NMR, prokaryotic in-cell NMR, particularly employing commonly used protein overexpression systems in Escherichia coli cells, is the most accessible approach. In this chapter we describe general procedures for obtaining in-cell NMR spectra in E. coli cells. |
| Volume | 895 |
| Pages | 19-31 |
| Published | 2012-1-1 |
| DOI | 10.1007/978-1-61779-927-3_2 |
| PMID | 22760309 |
| MeSH | Culture Techniques Escherichia coli / chemistry* Escherichia coli / metabolism Isotope Labeling Nuclear Magnetic Resonance, Biomolecular* Prokaryotic Cells / metabolism Protein Conformation Recombinant Proteins / biosynthesis Recombinant Proteins / chemistry |
| Altmetric score |
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| The most frequently cited source | F1000Research |
| Total number of mentions | 1 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| DNA material | Thermus thermophilus expression plasmid TEx14F08 (THR005728) TEx02C08 (THR000856) TEx16E07 (THR006503). |