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Brinker, A., Pfeifer, G., Kerner, M.J., Naylor, D.J., Hartl, F.U. and Hayer-Hartl, M. (2001) Dual function of protein confinement in chaperonin-assisted protein folding. Cell, 107, 223-233. doi:10.1016/S0092-8674(01)00517-7

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• TITLE: High yield expression of proteins in E. coli for NMR studies

  AUTHORS: Somnath Mondal, Divya Shet, Chinmayi Prasanna, Hanudatta S. Atreya

  KEYWORDS: E. Coli; Recombinant DNA Technology; Structural Biology; NMR Spectroscopy

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.6, June 24, 2013

  ABSTRACT: In recent years, high yield expression of proteins in E. coli has witnessed rapid progress with developments of new methodologies and technologies. An important advancement has been the development of novel recombinant cloning approaches and protocols to express heterologous proteins for Nuclear Magnetic Resonance (NMR) studies and for isotopic enrichment. Isotope labeling in NMR is necessary for rapid acquisition of high dimensional spectra for structural studies. In addition, higher yield of proteins using various solubility and affinity tags has made protein over-expression cost-effective. Taken together, these methods have opened new avenues for structural studies of proteins and their interactions. This article deals with the different techniques that are employed for over-expression of proteins in E. coli and different methods used for isotope labeling of proteins vis-à-vis NMR spectroscopy.