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NMR spectrometer has been regarded as essential tool for structure elucidation in variable scientific field as like organic synthesis, natural product and macro protein research. Also NMR can be applied for defining dynamic behavior like ligand and receptor binding. One of advantage of research with NMR is that to be great confident to confirm structure and the measured sample could be recovered. Nevertheless NMR also has a weak points than other spectroscopic methods that require a lot of time for interpreting acquired spectrum and running time due to low sensitivity. For last two decade Bruker has developed hardware and software solution for overcome those weak points. In order to overcome low sensitivity Bruker introduced Cryo and Micro diameter probe head technology. And researcher can reduce the time for routine spectrum processing and interpretation works due to lots of introductions in software solutions for quantification, identification and statistics analysis. With four examples, this article describing those new hardware and software solutions in field of recent pharmaceutical research as follows. - New Horizons for NMR in the Biopharmaceutical Industry - The development and application of solid-state NMR spectroscopy (SSNMR) in pharmaceutical analysis - Assisted NMR Data Interpretation in Synthetic Chemistry - Complete Analysis of New Psychoactive Substances Using NMR.
Bean sprouts are often cultivated in the circumstances prevailing in the improper using of germicide and growth enhancer. The influence of ingestion those bean sprouts are unknown. The components of the bean sprouts are needed to evaluate for food safety. The extracts of the control, 0.5 g/L germicide, 1 g/L germicide, 12.5 mL/L growth enhancer and 25 mL/L growth enhancer were used to compare the components in the experiment. Nuclear Magnetic Resonance spectroscopy (NMR) was used to analyze the extracts. Statistical analysis of metabolomics showed significant changes between the control and head and the stem of the bean sprouts. Significant changes in metabolites were identified with the bean sprouts cultivated with germicide and growth enhancer by applying qualitative and quantitative analysis. Similar changes in the area of the bean sprouts were observed after treated to germicide and growth enhancer. Although treating germicide and growth enhancer showed no particular harmful metabolites changes to human, it made significant changes in the morphological and the metabolites of the bean sprouts. These changes indicate that the germicide and growth enhancer has substantially potential to influence the growth of the bean sprouts.
Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.
Resonance frequencies from the 113Cd and 133Cs nuclear magnetic resonance (NMR) spectra for the CsCdBr3 single crystal were measured at varying temperatures by the static NMR method. The temperature-dependent changes of these frequencies are related to the changing structural geometry of the CdBr64‒ units, which affects the environment of 133Cs. The spin-lattice relaxation rates (1/T1) for the 113Cd and 133Cs nuclei were measured in order to obtain detailed information about the dynamics of CsCdBr3 crystals. The dominant relaxation mechanisms for 113Cd and 133Cs nuclei are direct single-phonon and Raman spin-phonon processes, respectively.
The cytoplasmic domains A and B of the mannitol transporter enzyme IIMtl are covalently linked in Escherichia coli, but separately expressed in Thermoanaerobacter Tengcongensis. The phosphorylation of domain B (TtIIBMtl) substantially increases the binding affinity to the domain A (TtIIAMtl) in T. Tengcongensis. To understand the structural basis of the enhanced domain-domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho-TtIIBMtl using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.
Cupin-superfamily proteins represent the most functionally diverse groups of proteins and include a huge number of functionally uncharacterized proteins. Recently, YaiE, a cupin protein from Escherichia coli has been suggested to be involved in a novel activity of pyrimidine/purine nucleoside phosphorylase (PPNP). In the present study, we achieved a complete backbone NMR assignments of YaiE, by a series of heteronuclear multidimensional NMR experiments on its [13C/15N]-enriched sample. Subsequently, secondary structure analysis using the assigned chemical shift values identified 10 obvious β-strands and a tentative 310-helix. Taken all together, the results constitute the first structural characterization of a putative PPNP cupin protein.
Metabolomics is one of latest '-omics', which is to analyze metabolome in cells, tissues and biofluids and to study metabolisms. It has become increasingly popular since 1990. The first goal of metabolomics is to analyze metabolites in a technical aspect. The major two analytical platforms in metabolomics are NMR spectroscopy and mass spectrometry (MS). MS is superior to NMR for detecting many more metabolites. That is one of the most important factors in metabolomics. However, NMR also has several advantages over MS. In this review, I firstly introduced metabolomics by comparing NMR-based metabolomics and MS-based metabolomics. Second, I explored technical issues on sample preparation and NMR experiments for metabolite identification and quantification.
Escherichia coli responds to ever-changing external and internal stresses by rapidly adjusting its physiology for better survival. This adjustment occurs at all levels including metabolites as well as mRNAs and proteins. Although there has been many reports describing E. coli's adaptation to various stresses regarding transcriptomics or proteomics, only a few investigations have been reported regarding this adaptation viewed from metabolites' perspective. We applied four different types of stresses at four different doses as imposed by NaCl, sorbitol, ethanol, and pH to investigate the similarities or differences among the stresses, and which stress causes the largest perturbation of the metabolite composition. We profiled the metabolites under such external stresses by using two-dimensional NMR spectroscopy and identified 39 metabolites including amino acids, sugars, organic acids, and nucleic acids. According to our statistical analysis, the osmotic stress caused by sorbitol differentiated itself from others, while NaCl showed the largest dose dependent metabolic perturbations. We hope this work will form a foundation on which an approach to a successful protein production is systematically provided by a favorable metabolic environment by imposing proper external stresses.
The 14N NMR spectra for (NH4)2SO4 crystals were obtained near the phase transition temperature TC=223 K, and were found to precisely reflect the symmetry change in the crystal at this first-order phase transition. Changes in the resonance frequencies near TC were attributed to the structural phase transition. In the ferroelectric and paraelectric phases, two inequivalent NH4 groups were distinguished in the 14N NMR spectra. The two types, NH4(1) and NH4(2), have slightly different local environments. Consequently, we conclude that the phase transition is caused by the change in the environment of the 14N nuclei in the NH4 groups, rather than by the SO4 groups.
It is now well established that RNAs exhibit fundamental roles in regulating cellular processes. Many of these RNAs do not exist in a single conformation. Rather, they undergo dynamic transitions among many different conformations to mediate critical interactions with other biomolecules such as proteins, RNAs, DNAs, or small molecules. Here, we briefly review NMR techniques that describe the dynamic behavior of RNA by determining structural, kinetic, and thermodynamic properties.