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Isotope Labeling Methods for Relaxation Measurements

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Isotope labeling in Biomolecular NMR

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 992))

Abstract

Nuclear magnetic spin relaxation has emerged as a powerful technique for probing molecular dynamics. Not only is it possible to use it for determination 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 15N labeled samples have been used for these experiments but it is clear that this limits the applications. For instance, sensitivity for large systems is dramatically increased if dynamics is probed at methyl groups and structural characterization of low-populated states requires measurements on 13Cα, 13Cβ or 13CO or 1Hα. Unfortunately, homonuclear scalar couplings may lead to artifacts in the latter types of experiments and selective isotopic labeling schemes that only label the desired position are necessary. Both selective and uniform labeling schemes for measurements of relaxation rates for a large number of positions in proteins are discussed in this chapter.

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  1. Division of Molecular Biotechnology, Department of Physics, Chemistry and Biology, Linköping University, SE-58183, Linköping, Sweden

    Patrik Lundström, Alexandra Ahlner & Annica Theresia Blissing

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  1. Patrik Lundström
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  2. Alexandra Ahlner
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Correspondence to Patrik Lundström .

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  1. , NMR Research Centre, Indian Institute of Science, Bangalore, India

    Hanudatta S. Atreya

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Lundström, P., Ahlner, A., Blissing, A.T. (2012). Isotope Labeling Methods for Relaxation Measurements. In: Atreya, H. (eds) Isotope labeling in Biomolecular NMR. Advances in Experimental Medicine and Biology, vol 992. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4954-2_4

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