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


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

Cite this paper

Mondal, S. , Shet, D. , Prasanna, C. and Atreya, H. 2013 High yield expression of proteins in E. coli for NMR studies. Advances in Bioscience and Biotechnology, 4, 751-767. doi: 10.4236-abb.2013.46099.

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

Fuente: http://www.scirp.org/


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