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Updated: Aug 9, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

サイト・ディレクテッド・パラレル・スピン・ラベリングとパラマグネティック・リラクゼーション・エンハンスメントは,溶液NMRスペクトロスコピーによる膜タンパク質の構造決定に用いられる

Binyong Liang1, John H Bushweller, Lukas K Tamm

  • 1Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, 22908-0736, USA.

Journal of the American Chemical Society
|March 30, 2006
PubMed
まとめ

NMRで統合膜タンパク質の構造を決定することは困難です. この研究では,限界を克服するために並列スピンラベルを導入し,構造計算を改善するために正確な距離測定を可能にします.

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Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
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When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
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