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Nuclear Magnetic Resonance:     more books (100)

Nuclear Magnetic Resonance Imaging in Medicine Nuclear Magnetic Resonance Spectra of Simple Heterocycles (General heterocyclic chemistry series) by T.J. Batterham, 1973-09 Nuclear Magnetic Resonance Data Book for Biomedical Applications by P.T. Beall, etc., 1984-12-01 Nuclear magnetic resonance studies in lyotropic liquid crystals (NMR) by C L; Kunwar, A C; Tracey, A S; Diehl, P Khetrapal, 1975 Nuclear Magnetic Resonance in Biology Frontiers of Nuclear Magnetic Resonance in Molecular Biology (UCLA Symposia on Molecular and Cellular Biology, New Series) by David Live, etc., 1990-03-21 Interpreting Infrared, Raman, and Nuclear Magnetic Resonance Spectra ( 2 volume set) (Vol 1) by Richard A. Nyquist, 2001-04-20 Nuclear Magnetic Resonance (SPR Nuclear Magnetic Resonance) (Vol. 35) Nuclear Magnetic Resonance in Biochemistry: Applications to Enzyme Systems by Raymond A. Dwek, 1973-12-13 Nuclear Magnetic Resonance (Documents on Modern Physics) by Francis A. Rushworth, 1973-12 Nuclear Magnetic Resonance, Part C, Volume 239 (Methods in Enzymology) Progress in Nuclear Magnetic Resonance Spectroscopy by J. W. Emsley, 1984-09 Progress in nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance of Liquid Crystals (NATO Science Series C: (closed))

lists with details

81. Nuclear Magnetic Resonance Core Facility - Standard Operating Procedures
    nuclear magnetic resonance CORE FACILITY. PART I DESCRIPTION OF SERVICES. Introduction The applications for solution NMR have greatly  
    http://www.med.cornell.edu/research/cores/core10/sop.html
    
    Extractions: CORE FACILITY Introduction The applications for solution NMR have greatly expanded from a traditionally analytical technique to powerful biological tool for the investigation of biomolecule structure, dynamics, and stability. A wide variety of experiments exist for analyzing biological molecules using NMR. Basic 1D and 2D applications can often be employed on small proteins and other compounds in a matter of hours to assess: composition, structure, sample purity, mutational effects and ligand binding interactions. More involved multidimensional NMR applications can be employed for protein structure determination and dynamics investigations. Collaborations. The variety of NMR applications require differing levels of expertise for collecting and analyzing the NMR data. Collaborations with NMR facility members may be advised, depending upon the expertise of the user. Co-authorship of potential manuscripts should be discussed at an early stage in projects. Assisted and Unassisted NMR use. Users are encouraged to learn NMR data collection and processing techniques. Training sessions on the basic use of the NMR spectrometer will be offered at intervals throughout the year for new users. Only trained users will be allowed to independently operate the NMR spectrometer.

82. Nuclear Magnetic Resonance Research (NMR)
    For those studies, we use nuclear magnetic resonance spectroscopy and follow the behavior of the drugs in human colon cancers growing in mice.  
    http://mayoresearch.mayo.edu/mayo/research/nmr/
    
    Extractions: Medical Services Jobs News Faculty Contact Personnel Services Nuclear Magnetic Resonance Research (NMR) ... Printable Version The NMR Facility at Mayo currently supports three main fields of NMR biomedical application: Study of the structure of biomacromolecules in solution by high field, high resolution NMR spectroscopy: At present, NMR spectroscopy is the only technique that can provide detailed solution structure of small proteins and polynucleotides. NMR spectroscopy of small laboratory animals ( in vivo NMR) and cell cultures: Due to the noninvasive character of the main interactions, NMR is very suitable for in vivo studies. It provides information on the composition and concentration of metabolites in body fluids, cells, tissues, and organs. In vivo NMR spectra are very useful for monitoring subtle metabolic changes. NMR imaging of small laboratory animals: The NMR experiment, when performed in a magnetic field with a controlled gradient, provides spatial distribution of observed spins, i.e. the NMR image, rather than NMR spectrum. The NMR images give noninvasive pictures of cross-sections of biological objects. Combined with spectroscopy, NMR images give a detailed map of the physiological state of a studied model. For example, we are currently investigating how the drug levamisole helps the drug 5-FU extend the life of some patients who have undergone surgery for colon cancer. For those studies, we use nuclear magnetic resonance spectroscopy and follow the behavior of the drugs in human colon cancers growing in mice. We are monitoring the nuclear magnetic resonance signal of phosphorous and fluorine nuclei in tumor xenografts in mice. Phosphorous is a natural part of living systems. Fluorine is a major component of the drug 5-FU. By phosphorous NMR, we follow the viability of tumor cells and by fluorine NMR, the concentration and metabolism of the added drug 5-FU. The results of these studies will help determine how the two drugs interact in the body and may eventually lead to further improvements in therapy.

83. Nuclear Magnetic Resonance Spectroscopy - RTI International
    nuclear magnetic resonance Spectroscopy RTI International - Advanced capabilities for measuring chemical compounds and isotopes.  
    http://www.rti.org/page.cfm?nav=303

84. Biophysical Chemistry - Nuclear Magnetic Resonance
    Biophysical Chemistry. nuclear magnetic resonance Application and development of NMR methodology and theory. The nuclear magnetic  
    http://www.fkem2.lth.se/research/areas/nmr.html
    
    Extractions: Application and development of NMR methodology and theory The nuclear magnetic resonance phenomenon underlies a large and growing family of experimental techniques for investigating the structure, dynamics and interactions of condensed matter on length scales from the molecular to the macroscopic, and on time scales from picoseconds to hours and longer. Forty years ago, when NMR had become an established method in chemical research, about 2,000 papers had been published in the NMR field. Today, a similar number of NMR papers are added to the literature every five weeks in fields ranging from solid-state physics to neurophysiology. No other physical probe of molecular behavior can rival NMR in range of applications and potential for development. During the past two decades, the biomolecular and medical applications of NMR have been transformed by major methodological breakthroughs and today they dominate the field. NMR is used in one way or another in the majority of the biophysical research projects undertaken in the Department. We use NMR to determine the three-dimensional structures of proteins in solution, to characterize conformational dynamics essential for protein function, and to study the interactions of proteins and nucleic acids with other molecules, including water, co-solvents and ions, functional ligands and other biomolecules.

85. RMN - A Nuclear Magnetic Resonance Data Processing Program.
    RMN is a nuclear magnetic resonance (NMR) data processing program for the Macintosh. Download the latest binhexed version of the program!  
    http://www.chemistry.ohio-state.edu/~grandinetti/RMN/

86. Vls.icm.edu.pl/cgi-bin/sciserv.pl?collection=elsevier Journal=00796565
    PDF Principles of nuclear magnetic resonancePage 1. Biomedical Imaging HET408 Principles of nuclear magnetic resonance April 24, 2002 Page 2. 1 The magnetic dipole moment of  
    http://vls.icm.edu.pl/cgi-bin/sciserv.pl?collection=elsevier&journal=00796565

87. NMR & X-ray Crystallography Glossary
    nuclear magnetic resonance Spectroscopy, DOE Genomes to Life, US http//www.doegenomestolife.org/technology/nmrspectroscopy.html.  
    http://www.genomicglossaries.com/content/nmr_email.asp
    
    Extractions: Registration policy has details Mr. Ms. Mrs. Dr. Prof. First: Last: Title: Dept.: Company: Address: City: State: Zip: Country: Email: Opt-out of Email YES NO Telephone: Fax: document.FrontPage_Form1.interest.value = 'NMR PST'; N uclear magnetic resonance (NMR) spectroscopy uses high magnetic fields and radio- frequency pulses to manipulate the spin states of nuclei — including 1H, 13C, and 15N — that have nonzero- spin angular momentum. For a molecule containing such nuclei, the result is an NMR spectrum with peaks whose positions and intensities reflect the chemical environment and nucleic positions within the molecule. As applied to protein- structure analysis, the accuracy now achievable with NMR spectroscopy is comparable to that obtained with X-ray crystallography. Nuclear Magnetic Resonance Spectroscopy, DOE Genomes to Life, US http://www.doegenomestolife.org/technology/nmrspectroscopy.html

88. Nuclear Magnetic Resonance - CCSG
    . Mass Spectrometry. •. nuclear magnetic resonance. •. Microarray. •. . Prevention. nuclear magnetic resonance. Darrell Davis, Ph.D. Facility Director.  
    http://www.huntsmancancer.org/5255.html

89. UCLA-DOE Nuclear Magnetic Resonance (NMR) Core Facility
    UCLADOE nuclear magnetic resonance (NMR) Core Facility. Co-director Robert Clubb, 656 MBI, rclubb@mbi.ucla.edu. Co-director Juli  
    http://www.doe-mbi.ucla.edu/Facilities/nmr.html
    
    Extractions: Facilities and Equipment NMR Instrumentation. The facility contains three high field NMR spectrometers. All three spectrometers are equipped with multiple radiofrequency channels and three-axis field gradients and can perform almost all of the current, multi-dimensional, homo- and heteronuclear NMR experiments. The facility also contains various small equipment to enable the preparation of samples and the modification of solution conditions without the need to return to the main laboratories. This equipment includes a pH-meter, temperature controlled water bath, magnetic stirrer with heating plates, and pipetting equipment.

90. The Nuclear Magnetic Resonance Society Of Japan
    http://wwwsoc.nii.ac.jp/nmr/index-e.html

91. Nuclear Magnetic Resonance Spectroscopy
    David Morrissey 2001. nuclear magnetic resonance spectroscopy.  
    http://www.bch.bris.ac.uk/staff/pfdg/teaching/nmr.htm
    
    Extractions: David Morrissey Nuclear Magnetic Resonance spectroscopy Introduction Basics Shielding and spin coupling Fourier transform ... Structure assignment Introduction bacteriorhodopsin was determined. X-ray crystallography gives a 3D electron density map of a protein. The backbone structure is then fitted into this data as well as possible. NMR is a very different method, which uses radio frequency radiation to cause transitions between nuclear energy levels. The spectroscopic data gained effectively gives a (very large) set of restraints on the relative positions of the hydrogens. This will be explained later. Some nuclei have a quantum mechanical property called spin. For protons, there are two possible spin states (for simplicity, we'll call them up and down). This spin of a charged nucleus produces a magnetic field, and a magnetic moment which points along the axis of rotation. When there is no external magnetic field present, there is essentially no difference between up and down spin states, but if a magnetic field is applied then the nucleus can align so that it's magnetic moment points in the same direction as the magnetic field, or in the opposite direction. It is energetically more favourable for the magnetic moment (µ) to point in the same direction as the applied field (B ), so more nuclei will align this way than against the field. However, the difference between these energy levels is tiny even in strong magnetic fields, so that the excess number of spins in the lower energy state is very small. In addition to spinning, the nucleii precess, which is the rotation of the magnetic moment around an axis, as shown below. The behaviour is much like that of a spinning top.

92. Solid-State NMR Spectroscopy
    SolidState nuclear magnetic resonance. Welcome to the Laboratorium für Physikalische Chemie, Solid-State NMR Spectroscopy at the  
    http://www.nmr.ethz.ch/
    
    Extractions: Solid-State Nuclear Magnetic Resonance We are a research group in the which is part of the Department of Chemistry and Applied Biosciences of the . This research group is led by Professor Dr. Beat Meier. Area of Research Publication List of Prof. Beat H. Meier Available Instrumentation Links to Other Research Groups ...

93. 1998 Building Publications - H Nuclear Magnetic Resonance Characterization Of Po
    Water molecular dynamics in a hardened Portland cement were characterized by proton Fourier transform nuclear magnetic resonance (NMR) at 400MHz.  
    http://fire.nist.gov/bfrlpubs/build98/art074.html

94. UW Centres, Institutes, Research Groups, & Centres Of Excellence
    people forms policies/procedures research home UW home. Waterloo nuclear magnetic resonance Centre. Contact Dr. Hartwig Peemoeller, Director. Department Physics.  
    http://www.research.uwaterloo.ca/main/cirg/cirg_template.asp?group=35

95. Michael F. Summers
    Michael Summers is interested in the application of nuclear magnetic resonance to studies of the structure and function of proteins, RNA, and macromolecular  
    http://www.hhmi.org/science/strucbio/summers.htm
    
    Extractions: Summary: Michael Summers is interested in the application of nuclear magnetic resonance to studies of the structure and function of proteins, RNA, and macromolecular interactions. Nuclear magnetic resonance (NMR) and computational methods are employed in our laboratory to address protein-protein and protein-RNA interactions that occur as retroviruses assemble in infected cells. Recently we have focused on the Gag proteins from the human immunodeficiency virus (HIV) and the Moloney murine leukemia virus (MoMuLV), and the interactions between these proteins and their cognate Y -RNA recognition elements. We have also focused on the identification of new classes of antiviral compounds that inhibit these interactions. All retroviruses encode a Gag precursor polyprotein that functions in the recognition of viral RNA and in the assembly of virus particles. Subsequent to budding, the Gag polyproteins are processed by the viral protease to smaller proteins, including the nucleocapsid (NC p7), capsid (CA p24), and matrix (MA p17) proteins. The capsid proteins assemble during this maturation process to form the capsid core in the center of the virus that encapsidates the viral RNA.

96. IBM Research | Almaden Research Center | Science And Technology | Scientific Ser
    IBM Research Almaden Research Center Science and Technology Scientific Services Materials Analyis nuclear magnetic resonance Analysis.  
    http://www.almaden.ibm.com/st/scientific_services/materials_analysis/nmr/
    
    Extractions: Overview The mission of the Almaden Research Center NMR Facility is to develop new measurement techniques and to provide a limited routine service for applications of NMR spectroscopy in the area of information technology related materials problems. At ARC, NMR spectroscopy is used for structure determination/characterization relating to the following materials problems: Photolithographic Systems This class of materials includes the polymers, photo-acid generators, small-molecule additives, and casting solvents that make up a photoresist. Quantitative solution-state 13C NMR allows for total component analysis of both bulk resist solutions and processed thin films. Polymeric Dielectric Materials Solid-state NMR techniques such as combined Cross-Polarization and Magic-Angle Spinning (CPMAS) are particularly important for the characterization of these materials due to their insolubility in final cured form. NMR spectroscopy is one of the few techniques that can give information on the microscopic chemical structure of these materials as a function of processing conditions. Head/Disk Interface Materials Amorphous carbon overcoats and perfluoropolyether lubricants are included in this class of materials. Solid-state 13C NMR has been used to learn about structural variations in amorphous CHx films as a function of sputter conditions. The composition, molecular weight, and decomposition products of perfluoropolyethers can be determined using solution-state 19F NMR techniques.

97. Elsevier Author Gateway
    Solid State nuclear magnetic resonance, Firsttime author? user name password  
    http://authors.elsevier.com/JournalDetail.html?PubID=622947&Precis=DESC

98. Wiley::Encyclopedia Of Nuclear Magnetic Resonance, Volume 9, Advances In NMR
    Wiley Chemistry Spectroscopy NMR Spectroscopy Encyclopedia of nuclear magnetic resonance, Volume 9, Advances in NMR.  
    http://www.wiley.com/WileyCDA/WileyTitle/productCd-0471490822.html

99. Wiley::Encyclopedia Of Nuclear Magnetic Resonance, 8 Volume Set
    By Keyword, Wiley Chemistry Spectroscopy NMR Spectroscopy Encyclopedia of nuclear magnetic resonance, 8 Volume Set.  
    http://www.wiley.com/WileyCDA/WileyTitle/productCd-0471938718.html

100. References
     nuclear magnetic resonance Quantum Computers. .Quantum computers have the potential to revolutionise many branches of science through  
     http://www.qubit.org/research/NMR/
     
     Extractions: Nuclear Magnetic Resonance Quantum Computers Quantum computers have the potential to revolutionise many branches of science through their ability to tackle problems too large for any classical computer. While the theory of quantum computing is well understood, actually building a quantum computer has proved extremely difficult. Several approaches have been studied, but until recently it has only been possible to demonstrate the very simplest operations. In the last few years, however, the development of computers based on Nuclear Magnetic Resonance (NMR) spectroscopy has been extremely rapid. Researchers at IBM, MIT and Berkeley and in our laboratory in Oxford have recently demonstrated powerful quantum search algorithms using small NMR computers. The H and NMR computers are different from other quantum computers in one important respect. The NMR signal from a single molecule is far too weak to be detected, and so it is necessary to use a large number of identical copies to amplify the signal. This is not difficult as even a few milligrams of a chemical compound will contain the required number of molecules. It is however impossible to ensure that all the copies start the calculation in the same initial state, and so different copies will in effect perform different calculations, making it extremely difficult to extract the desired result. This inability to prepare NMR computers in a well defined initial state prevented their use for many years.

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