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A significant part of the progress observed in scientific areas like Chemistry, Biology or Medicine can be ascribed to the development experienced by NMR in recent times. Many of the books currently available on NMR deal with the theoretical basis and some of its main applications, but they generally demand a strong background in Physics and Mathematics for a full understanding. This book is aimed to a wide scientific audience, trying to introduce NMR by making all possible effort to remove, without losing any formality and rigor, most of the theoretical jargon that is present in other NMR books.

Furthermore, illustrations are provided that show all the basic concepts using a naive vector formalism, or using a simplified approach to the particular NMR-technique described. The intention has been to show simply the foundations and main concepts of NMR, rather than seeking thorough mathematical expressions.

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Vibrational Spectroscopy at Electrified Interfaces. Doping in Conjugated Polymers. Pradip Kar. Csaba Visy. Single-Molecule Electronics. Manabu Kiguchi. Observing the change in peak position and linewidths as a function of temperature or the determination of the coalescence temperature allows extracting the reaction rates and the activation energy for the exchange process.

Applications in Life Science and Biochemistry The usefulness of NMR is increasingly being recognized in biology and biochemistry as well.

An introduction to biological NMR spectroscopy.

The determination of a protein structure is a considerable task, and often such a project, depending on the size of the protein and how well-behaved it is, can take a few years. The time-consuming step is the assignment of chemical shifts using data from 3D triple-resonance experiments. Structures of proteins exceeding 40 kDa are usually tough projects and require producing a lot of specially labeled protein samples.

One can resort to 15 N labeling even for small proteins say even less then 50 residues, if there is a route for recombinant production , 15 N, 13 C double labeling in the range of residues, while deuteration is required for those that are even larger. Figure 3 shows an example from research at UZH: It was discovered that the designed Armadillo repeat protein of the YM 3 A type, in which Y and A denote the N- and C-terminal caps and M the three internal identical repeats, can be reconstituted from two complementary fragments. The spectrum of YM2 on the top left clearly resembles a molten-globule type protein, and adding the unlabeled MA fragment converts that spectrum into one of a properly folded protein.

The structure of the complex was determined based on NOEs. Advances in spectroscopy have pushed the size-limit considerably. A major breakthrough was the development of the so-called TROSY-type pulse sequences [9], that allow to largely reduce the impact of the direct dipolar coupling for relaxation.

NMR Spectroscopy - The Chemical Shift

To be most efficient all other protons should be removed by deuteration [10]. While this is certainly something for a highly specialized lab, the take home message here is that recording 15 N- 1 H or 13 C- 1 H for methyl groups correlation experiments are possible even for large proteins. Assigning them will be difficult, but sometimes this is not necessary, e.

In fact, there are a number of biochemical problems that do not require extensive NMR expertise but just access to a spectrometer and a couple of hours of measuring time! Even for the non-professional there is a lot to be discovered from simple protein NMR spectra: The chemical shift dispersion in 1D proton spectra will report on whether a protein is folded or not, and whether it is well-behaving non-aggregating at NMR concentrations.

Signals from flexible residues are much more intense for large proteins. A typical question could be whether the expressed protein construct contains long flexible tails that hamper crystallization. If the protein can be produced in 15 N-labeled form a proton-nitrogen correlation map will even allow to quickly identify flexible parts and their location. When the protein is produced in E. The backbone dynamics data are derived from 15 N relaxation experiments. The data analysis is rather straightforward, and it adds valuable data to the function-dynamics topic.

Even in the absence of assignments this experiment will immediately reveal whether flexible tails or long flexible loops are present and thereby help to eliminate or truncate such flexible moieties. Another question of interest often is whether the protein interacts with a small molecule, a typical question in drug-discovery [15,16]. In contrast to biochemical assays only two components exist in the NMR experiment, and if pH, salt content and temperature are tightly controlled, no false-positive will be seen.

In the protein-observe methods the protein is usually 15 N labeled. When adding the small molecule, peaks from residues in contact with the ligand will shift, indicating that the small molecule binds to the protein. If assignments already exist, the binding site can be rapidly identified. The advantage of the ligand-observe techniques is that no labeled protein is required.

The saturation-transfer difference experiment STD [17] has become popular to detect binding on the ligand. The experiment is very simple to perform, and it works very well in presence of large receptor proteins. Moreover, RNA can be labeled at comparably low cost. The determination of RNA structure has become routine nowadays [18], and procedures for structure determination are very similar to those used for proteins. Another field from the life science area that has attracted some attention is metabolomics [19]. In metabolomics the presence of metabolites in biological fluids, e.

A maximum of 5 trainees will be in a session.

An introduction to biological NMR spectroscopy.

Magnet: Console: 4 channels. Software: Topspin 3. Application: proteins, liquids and solids. Book Here. System: Avance III. Application: proteins. Probe: TXI probe; 1. Application: proteins, solid-state NMR. Magnet: 9.