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Heteronuclear single-quantum correlation spectroscopy (HSQC) is a 2D NMR technique that reveals one-bond correlations between hydrogen and a heteronucleus. The HSQC experiment is similar to the heteronuclear correlation experiment (HETCOR) but is more sensitive. In the HSQC spectrum, the proton chemical shift is plotted on the horizontal F2 axis, while the 13C chemical shift is plotted on the vertical F1 axis. The corresponding proton and 13C spectra are also shown. The HSQC contour plot does...
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Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
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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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Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
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NMR Spectroscopy: Chemical Shift Overview01:15

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The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
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When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.

Chaowei Shi1, Hannes K Fasshuber, Veniamin Chevelkov

  • 1Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.

Journal of Biomolecular NMR
|March 4, 2014
PubMed
Summary
This summary is machine-generated.

Band-selective homonuclear cross-polarization (BSH-CP) enhances carbon-carbon (CO-CA) transfer in solid-state NMR (ssNMR). This method enables rapid protein resonance assignment using 3D ssNMR, potentially replacing existing techniques.

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Area of Science:

  • Solid-state Nuclear Magnetic Resonance (ssNMR) Spectroscopy
  • Protein Structure and Dynamics
  • Biomolecular NMR Spectroscopy

Background:

  • Efficient magnetization transfer is crucial for resonance assignment in solid-state NMR (ssNMR) of proteins.
  • Current CO-CA (carbonyl-to-alpha carbon) transfer methods can be time-consuming and less efficient.
  • Band-selective homonuclear cross-polarization (BSH-CP) has shown promise for improved CO-CA transfer.

Purpose of the Study:

  • To integrate the BSH-CP technique into established 3D ssNMR pulse schemes.
  • To evaluate the efficiency and speed of BSH-CP for protein resonance assignment.
  • To assess the potential of BSH-CP as a replacement for conventional CO-CA transfer methods.

Main Methods:

  • Incorporation of the BSH-CP CO-CA transfer block into 3D ssNMR pulse sequences.
  • Application of these modified pulse schemes to a model protein (ubiquitin) at high magnetic fields and moderate magic-angle spinning rates.
  • Measurement of CO-CA transfer efficiency and acquisition time for complete resonance assignment.

Main Results:

  • The BSH-CP block was successfully integrated into 3D ssNMR pulse schemes.
  • An excellent CO-CA transfer efficiency of 33% was achieved using BSH-CP.
  • A complete set of 3D spectra for unambiguous resonance assignment of ubiquitin was rapidly acquired within one week.

Conclusions:

  • BSH-CP is a highly efficient method for CO-CA transfer in solid proteins.
  • The integration of BSH-CP into 3D ssNMR enables rapid and unambiguous protein resonance assignment.
  • BSH-CP is a promising alternative to existing CO-CA transfer schemes in 3D ssNMR for biomolecular studies.