| Chapter title |
In-cell NMR of intrinsically disordered proteins in prokaryotic cells.
|
|---|---|
| Chapter number | 2 |
| Book title |
Intrinsically Disordered Protein Analysis
|
| Published in |
Methods in molecular biology, July 2012
|
| DOI | 10.1007/978-1-61779-927-3_2 |
| Pubmed ID | |
| Book ISBNs |
978-1-61779-926-6, 978-1-61779-927-3
|
| Authors |
Ito Y, Mikawa T, Smith BO, Yutaka Ito, Tsutomu Mikawa, Brian O. Smith |
| 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. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 1 | 6% |
| Portugal | 1 | 6% |
| Unknown | 16 | 89% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 6 | 33% |
| Student > Ph. D. Student | 5 | 28% |
| Professor | 2 | 11% |
| Student > Master | 2 | 11% |
| Lecturer | 1 | 6% |
| Other | 2 | 11% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 7 | 39% |
| Chemistry | 4 | 22% |
| Agricultural and Biological Sciences | 3 | 17% |
| Chemical Engineering | 1 | 6% |
| Unknown | 3 | 17% |