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Matches in DBpedia 2014 for { <http://dbpedia.org/resource/Nuclear_magnetic_resonance_spectroscopy_of_proteins> ?p ?o. }

• Nuclear_magnetic_resonance_spectroscopy_of_proteins abstract "Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.NMR involves the quantum mechanical properties of the central core ("nucleus") of the atom. These properties depend on the local molecular environment, and their measurement provides a map of how the atoms are linked chemically, how close they are in space, and how rapidly they move with respect to each other. These properties are fundamentally the same as those used in the more familiar Magnetic Resonance Imaging (MRI), but the molecular applications use a somewhat different approach, appropriate to the change of scale from millimeters (of interest to radiologists) to nano-meters (bonded atoms are typically a fraction of a nano-meter apart), a factor of a million. This change of scale requires much higher sensitivity of detection and stability for long term measurement. In contrast to MRI, structural biology studies do not directly generate an image, but rely on complex computer calculations to generate three-dimensional molecular models.Currently most samples are examined in a solution in water, but methods are being developed to also work with solid samples. Data collection relies on placing the sample inside a powerful magnet, sending radio frequency signals through the sample, and measuring the absorption of those signals. Depending on the environment of atoms within the protein, the nuclei of individual atoms will absorb different frequencies of radio signals. Furthermore the absorption signals of different nuclei may be perturbed by adjacent nuclei. This information can be used to determine the distance between nuclei. These distances in turn can be used to determine the overall structure of the protein.A typical study might involve how two proteins interact with each other, possibly with a view to developing small molecules that can be used to probe the normal biology of the interaction ("chemical biology") or to provide possible leads for pharmaceutical use ("drug development"). Frequently, the interacting pair of proteins may have been identified by studies of human genetics, indicating the interaction can be disrupted by unfavorable mutations, or they may play a key role in the normal biology of a "model" organism like the fruit fly, yeast, the worm C. elegans, or mice. To prepare a sample, methods of molecular biology are typically used to make quantities by bacterial fermentation. This also permits changing the isotopic composition of the molecule, which is desirable because the isotopes behave differently and provide methods for identifying overlapping NMR signals.".
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• Nuclear_magnetic_resonance_spectroscopy_of_proteins wikiPageExternalLink nmr-relax.com.
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• Nuclear_magnetic_resonance_spectroscopy_of_proteins subject Category:Biophysics.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins subject Category:Nuclear_magnetic_resonance.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins subject Category:Protein_methods.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins subject Category:Protein_structure.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins type Ability105616246.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins type Abstraction100002137.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins type Cognition100023271.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins type Know-how105616786.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins type Method105660268.
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• Nuclear_magnetic_resonance_spectroscopy_of_proteins comment "Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques.".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins label "Espectroscopia mediante resonancia magnética nuclear de proteínas".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins label "Nuclear magnetic resonance spectroscopy of proteins".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins label "Ressonância magnética nuclear de proteínas".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins label "Spettroscopia a risonanza magnetica nucleare di proteine".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins label "مطيافية الرنين المغناطيسي النووي للبروتين".
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs Espectroscopia_mediante_resonancia_magnética_nuclear_de_proteínas.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs Spettroscopia_a_risonanza_magnetica_nucleare_di_proteine.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs Ressonância_magnética_nuclear_de_proteínas.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs m.09shvp.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs Q864267.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins sameAs Q864267.
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• Nuclear_magnetic_resonance_spectroscopy_of_proteins depiction NMR_sample.JPG.
• Nuclear_magnetic_resonance_spectroscopy_of_proteins isPrimaryTopicOf Nuclear_magnetic_resonance_spectroscopy_of_proteins.