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  • Proteins
  • In 1990, Ad Bax and coworkers developed the triple resonance technology and experiments on proteins isotopically labelled with 15N and 13C, with the result that the spectra are dramatically simplified, greatly facilitating the process of resonance assignment, and increasing the size of the protein that may be determined by NMR. (wikipedia.org)
  • After returning to Switzerland, Wüthrich collaborated with, among others, Nobel laureate Richard R. Ernst on developing the first two-dimensional NMR experiments, and established the nuclear Overhauser effect as a convenient way of measuring distances within proteins. (wikipedia.org)
  • However, in large molecules such as proteins the number of resonances can typically be several thousand and a one-dimensional spectrum inevitably has incidental overlaps. (wikipedia.org)
  • chemists
  • Indeed, the sensitivity of NMR chemical shifts to the type and character of neighbouring atoms, combined with their reasonably predictable tendencies has made them invaluable for both deciphering and describing the structure of thousands of newly synthesized or newly isolated compounds Interestingly the same sensitivity to a variety of important protein structural features has made protein chemical shifts equally valuable to protein chemists and biomolecular NMR spectroscopists. (wikipedia.org)
  • CUNY established the Center as an institute in 1988 to unite the efforts of CUNY chemists, biologists, and psychologists researching biomolecular structure, interactions and their effects on gene function. (wikipedia.org)
  • SSNMR
  • Moreover, he develops methods to address challenging questions in structural biology where ssNMR can be applied with particular advantages, and have made particular contributions to the development of dynamic nuclear polarisation and proton detection using fast magic angle spinning. (wikipedia.org)
  • assignment
  • This limitation is due to the need to assign NMR signals from the large number of nuclei in the protein - in larger protein, the greater number of nuclei results in overcrowding of resonances, and the increasing size of the protein also broadens the signals, making resonance assignment difficult. (wikipedia.org)
  • This research later led to the complete assignment of resonances for among others the bovine pancreatic trypsin inhibitor and glucagon. (wikipedia.org)
  • structure
  • A novel off-resonance rotating-frame 15N NMR spin relaxation experiment is used to characterize conformational fluctuations with correlation times between 32 and 175 microseconds in the third fibronectin type III domain of human tenascin-C. Conformational fluctuations of contiguous regions of the beta-sandwich structure of the type III domain may represent collective motions, such as transient twisting or breathing of the beta-sheets. (duke.edu)
  • 1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function. (ac.be)
  • Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. (wikipedia.org)
  • It has been one of the major obstacles in efficient extraction of internuclear distances, which are crucial in the structural analysis of biomolecular structure. (wikipedia.org)
  • Nuclear Magnetic Resonance (NMR) Core Facility :home to two Bunker NMR spectrometers, an 800 MHz (18.8 teslas) and 600 MHz (14.1 teslas), used to determine molecular structure. (wikipedia.org)
  • typically
  • 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 nanometers (bonded atoms are typically a fraction of a nanometer apart), a factor of a million. (wikipedia.org)