Quantitation of Recombinant Protein in Whole Cells and Cell Extracts via Solid-State NMR Spectroscopy
Author:
Affiliation:
1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi4007034
Reference20 articles.
1. Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein That Includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and Structural Characterization of Purified and Membrane-Associated Fgp41
2. Miles, A. P. and Saul, A. (2009) inProtein Protocols Handbook,3rd ed., pp487–496,Humana,Totowa, NJ.
3. Fast Quantification of Recombinant Protein Inclusion Bodies within Intact Cells by FT-IR Spectroscopy
4. Native Conformation at Specific Residues in Recombinant Inclusion Body Protein in Whole Cells Determined with Solid-State NMR Spectroscopy
5. Solid-State REDOR NMR Distance Measurements at the Ligand Site of a Bacterial Chemotaxis Membrane Receptor
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5. Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR;Philosophical Transactions of the Royal Society B: Biological Sciences;2015-10-05
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