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Updated: Jul 8, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

7D APSY-NMRスペクトロスコピーによる溶性非球状タンパク質のシーケンス固有の共振配分

Sebastian Hiller1, Christian Wasmer, Gerhard Wider

  • 1Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland.

Journal of the American Chemical Society
|August 19, 2007
PubMed
まとめ

この研究は,展開されたタンパク質の迅速な原子解像度分析のための自動化されたNMR方法を導入しています. この技術は,ノングローブラータンパク質の研究を大幅に加速し,その構造と機能に関する新しい洞察を可能にします.

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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)

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In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
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Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
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