Titlebook: Isotope labeling in Biomolecular NMR; Hanudatta S. Atreya Book 2012 Springer Science+Business Media Dordrecht 2012 Biomolecular NMR.Geneti

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Isotope Labeling Methods for Relaxation Measurementson of time constant(s) for molecular reorientation but it can also be used to characterize internal motions on time scales from picoseconds to seconds. Traditionally, uniformly .N labeled samples have been used for these experiments but it is clear that this limits the applications. For instance, se

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Isotope Labeling and Segmental Labeling of Larger RNAs for NMR Structural Studies. Almost half of the RNA structures deposited in the Protein Data Bank were determined by NMR spectroscopy, whereas NMR accounts for only 11% for proteins. Recent improvements in isotope labeling of RNA have strongly contributed to the high impact of NMR in RNA structure determination. In this book

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Cell-Free Protein Synthesis Using , Cell Extract for NMR Studiess. As compared with conventional cellular expression systems, the scrambling and dilution of amino acids are highly suppressed in the cell-free reaction, allowing the production of proteins with a wide variety of residue and site-specific isotope labeling patterns. In this chapter, the procedure for

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Isotope Labeling in Insect Cellss with secondary modifications etc., which can often only be expressed in eukaryotic expression hosts. Although . is the organism of choice for expression of proteins in isotope labeled form for NMR studies, bacterial cells have limitations concerning their ability of producing soluble and well-fold

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Isotope Labeling Methods for Large Systems schemes that lead to increased sensitivity as well as improved spectral resolution and simplification. These are described and discussed in this chapter, focusing on labeling schemes for amide proton and methyl proton detected experiments. We also discuss labeling methods for other potentially useful positions in proteins.

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