Multidimensional NMR methods

T. Parella, 2D methods for the measurement of long-range proton-carbon coupling constants, in Multidimensional NMR Methods for the Solution State, G. A. Morris and J. W. Emsley (eds.), John Wiley Sons Ltd, Chichester, 2010, pp. 305-314. 

Numerous new developments and applications of solid state NMR techniques have emerged. Multidimensional NMR methods are able to probe connectivity patterns of zeolite framework structures and solve ambiguities in line assignments [27], high-resolution techniques for quadrupolar nuclei have been developed [31-34], and powerful double-resonance methods permit the study of spatial... 

Multidimensional NMR methods, combined with isotope labeling, can provide access to virtually every atom in a molecule, unique for protein structural studies. This not only allows characterization of the structure and interaction of proteins in their native milieu, but also provides unparalleled possibilities to obtain a complete atomic-level resolution picture of protein dynamics in a time range from picoseconds up to seconds, the range where most motions relevant to protein function take place. A significant number of 15N and 13C relaxation studies have been performed on a large number of proteins in the last... 

There are a large number of one- and multidimensional NMR methods available for solving different analytical problems. Typically, only a few standard NMR experiments are necessary for solving most process-related analytical problems (Table 12.1). These methods are all straightforward and easy to execute routinely. A repertoire of more complex methods can be found elsewhere.9... 

The simplest experiments are those that focus just on the ligand. These are typically used to determine solution conformations or 3D structures of ligands. Homonuclear1H II ) or 21) NMR experiments are used mainly here. At the other end of the scale, experiments to study the macromolecular binding partner often require labeled protein and multidimensional NMR methods, as indicated on the right-hand side of Fig. 1. Finally, many NMR experiments provide information... 

V Kanelis, JD Forman-Kay, LE Kay (2001) Multidimensional NMR methods for protein structure determination, IUBMB Life 52 (6) 291-302... 

Many NMR studies of nuclides of low sensitivity (nucleus X) that are spin coupled to protons are now carried out by indirect detection of the proton resonance, primarily by multidimensional NMR methods that we discuss later. For such detection to be effective for an X that is in low natural abundance (such as 13C) or is selectively enriched, it is essential to discriminate against the much larger signal arising from proton resonances of molecules with a nonmagnetic form of the nuclide (e.g., t2C).We describe here two simple ways to achieve such discrimination. 

The H has been the traditional nucleus for biological studies in the past decade and researchers have successfully utilized multidimensional NMR methods to assign spectra for proteins up to 30 kDa. Other nuclei such as C, N, and P have been used but their lower gyromagnetic ratios and/or natural abundances reduce sensitivity unless expensive isotopic enrichment methods are employed. An alternative nucleus for studies of biological materials is F. F NMR is a powerful technique due to several unique... 

F. M. Marassi, J. J. Gesell and S. J. Opella, Recent Developments in Multidimensional NMR Methods for Structural Studies of Membrane Proteins , p. 121... 

Combined use of high field, H/ C/ triple resonance and multidimensional NMR methods provides enormous spectral dispersion and... 

In this chapter, we describe a variety of methodologies for applying multidimensional NMR (mostly 2D- and some 3D-NMR) for the characterization of fluoropolymers. Space limitations preclude a comprehensive survey of the literature. Instead, a few of the primary methodologies are described involving combined use of multidimensional NMR methods for structure elucidation. Then, a selected group of papers were reviewed to illustrate the applications of these methodologies to the characterization of some of the most common classes of fluoropolymers, including homo- and copolymers with poly(vinylidene fluoride), fluorinated polyethers, fluori-nated ionomers, poly(vinyl fluoride) and its copolymers, and polytetrafluoroethylene (PTFE) and its copolymers. 

NMR spectroscopy has proved to be a powerful method for the elucidation of the structure of relatively small macromolecules (molecular weights of up to ca. 10,000 Da). In particular, this applies to RNA molecules for which X-ray crystallographic analyses are relatively rare, mainly due to difficulties with their crystallization. Under certain conditions a total structure elucidation of these (small) molecules in their native environment (aqueous solution) at atomic resolution is feasible by means of multidimensional NMR methods [4-10]. Moreover, even distinctly larger molecules, like whole tRNAs, can be at least partially cbar-acterized with reference to their structure, in particular secondary structure [11-14]. As detailed below, in certain cases NMR spectroscopy can also provide useful information for the... 

Recent Developments in Multidimensional NMR Methods for Structural Studies of Membrane Proteins... 

The extension of the multidimensional NMR approach to larger proteins was subsequently made possible by the development of 3D- and 4D-NMR techniques incorporating INEPT and HMQC pulse sequences that were applied to and N-labelled proteins. These latter developments were made at NIH by Bax and Clore and their co-workers. These multidimensional NMR methods provide the spectral simplification required to completely assign the spectra of proteins of up to 30 kDa and to determine their structures to a resolution similar to the... 

Gal M, Frydman L (2010) Multidimensional NMR methods for the solution state. In Morris GA, Emsley JW (eds) Encyclopedia of magnetic resonance, Chap. 3. Wiley, Chichester, UK... 

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