Nuclear magnetic resonance protein

Pielak GJ, Li CG, Miklos AC, Schlesinger AP, Slade KM, Wang GF, Zigoneanu IG (2009) Protein nuclear magnetic resonance under physiological conditions. Biochemistry-US 48 226, 9170... 

Membrane Protein Nuclear Magnetic Resonance Spectroscopy... 

J.R. Knowles enquiring as to needs for costly equipment in chemistry. In turn Knowles put the question to his college colleague, R.J.P. Williams, who had been working for some three years on protein nuclear magnetic resonance using the somewhat unsatisfactory Varian 220 MHz NMR carrier wave spectrometer (not a Fourier transform instrument) based, very inconveniently, for a while at Harwell and then at ICI near Runcorn. (This work developed... 

See also Capillary Electrophoresis Overview. Chir-optical Analysis. Liquid Chromatography Column Technology Mobile Phase Selection Reversed Phase Instrumentation Amino Acids. Mass Spectrometry Peptides and Proteins. Nuclear Magnetic Resonance Spectroscopy Techniques Nuclear Overhauser Effect. Proteins Traditional Methods of Sequence Determination Foods. 

The structures of proteins are the key data for understanding the functions of proteins. There are three main techniques for measuring the structures of proteins nuclear magnetic resonance (NMR), cryo-electron microscopy (cryo-EM) and protein crystallography (X-ray diffraction). The solved structures of macromolecules, including proteins, nucleic acids and their complexes, are deposited in the Protein Data Bank (PDB). Up to 23 June of 2009, a total of 58 414 structures of macromolecules had been released in the PDB, and these were mostly protein structures (Table 7.1). Among these structures, about 86% were determined by protein crystallography. 

Endo T., Oya, M., Tamiya, N. and Hayashi, K. (1987) Role of C-terminal tail of long neurotoxins from snake venoms in molecular conformation and acetylcholine receptor binding Protein nuclear magnetic resonance and competition binding studies. Biochemistry 26 4592-4598. 

Because this problem is complex several avenues of attack have been devised in the last fifteen years. A combination of experimental developments (protein engineering, advances in x-ray and nuclear magnetic resonance (NMR), various time-resolved spectroscopies, single molecule manipulation methods) and theoretical approaches (use of statistical mechanics, different computational strategies, use of simple models) [5, 6 and 7] has led to a greater understanding of how polypeptide chains reach the native confonnation. 

TF Flavel. An evaluation of computational strategies for use m the determination of protein structure from distance constraints obtained by nuclear magnetic resonance. Prog Biophys Mol Biol 56 43, 1991. 

M Vasquez, ElA Scheraga. Calculation of protein conformation by the build-up procedure. Application to bovine pancreatic trypsin inhibitor using limited simulated nuclear magnetic resonance data. J Biomol Struct Dyn 5 705-755, 1988. 

GM Clore, MA Robien, AM Gronenborn. Exploring the limits of precision and accuracy of protein structures determined by nuclear magnetic resonance spectroscopy. J Mol Biol 231 82-102, 1993. 

Wiithrich, K. Protein structure determination in solution by nuclear magnetic resonance spectroscopy. Science 243 45-50, 1989. 

Lazo ND, Meine JG, Downing DT (1995) Lipids are covalently attached to rigid corneocyte protein envelope existing predominantly as beta-sheets a solid state nuclear magnetic resonance study. J Invest Dermatol 105 296-300... 

The use of computer simulations to study internal motions and thermodynamic properties is receiving increased attention. One important use of the method is to provide a more fundamental understanding of the molecular information contained in various kinds of experiments on these complex systems. In the first part of this paper we review recent work in our laboratory concerned with the use of computer simulations for the interpretation of experimental probes of molecular structure and dynamics of proteins and nucleic acids. The interplay between computer simulations and three experimental techniques is emphasized (1) nuclear magnetic resonance relaxation spectroscopy, (2) refinement of macro-molecular x-ray structures, and (3) vibrational spectroscopy. The treatment of solvent effects in biopolymer simulations is a difficult problem. It is not possible to study systematically the effect of solvent conditions, e.g. added salt concentration, on biopolymer properties by means of simulations alone. In the last part of the paper we review a more analytical approach we have developed to study polyelectrolyte properties of solvated biopolymers. The results are compared with computer simulations. 

Metabolomics studies the entire metabolism of an organism. It is possible to consider characterising the complex pattern of cellular proteins and metabolites that are excreted in urine. Pattern recognition techniques of nuclear magnetic resonance spectra have been applied to determine the dose-response using certain classical liver and kidney toxicants (Robertson et al, 2000). This could well provide a signature of the functional state of the kidney, and perturbations in the pattern as a result of exposure to a chemical could be observed. But first it would be necessary to understand how compounds with known effects on the kidney affect these processes. 

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