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NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

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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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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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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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Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

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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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2D NMR: Overview of Homonuclear Correlation Techniques01:16

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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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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Protein resonance assignment by BSH-CP-based 3D solid-state NMR experiments: A practical guide.

Jutta Hoffmann1, Julia Ruta1, Chaowei Shi1

  • 1Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.

Magnetic Resonance in Chemistry : MRC
|November 7, 2019
PubMed
Summary
This summary is machine-generated.

This tutorial introduces a method for protein structure analysis using solid-state NMR (ssNMR) spectroscopy. It details a technique for assigning atomic resonances in proteins, crucial for understanding their structure and dynamics.

Keywords:
BSH-CPmagic-angle spinningprotein NMRresonance assignmentsolid-state NMR

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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Solid-state NMR (ssNMR) spectroscopy provides atomic-level structural and dynamic information for proteins.
  • It is particularly useful for insoluble or non-crystalline proteins unsuitable for X-ray crystallography or solution NMR.
  • Accurate chemical shift assignment of protein atoms is essential for ssNMR data analysis.

Purpose of the Study:

  • To provide a detailed tutorial on chemical shift assignment of protein backbone atoms.
  • To describe the application of band-selective homo-nuclear cross-polarization (BSH-CP) in 13C-detected ssNMR experiments.
  • To enable efficient and time-saving protein assignment for scientists with limited ssNMR experience.

Main Methods:

  • Utilizes 13C-15N-labeled proteins.
  • Employs a set of six 3D ssNMR experiments.
  • Incorporates band-selective homo-nuclear cross-polarization (BSH-CP) for magnetization transfer between carbonyl carbon (CO) and alpha carbon (CA) atoms.

Main Results:

  • Enables unambiguous assignment of protein backbone resonances.
  • Facilitates assignment of certain side-chain resonances.
  • Demonstrates an efficient approach for ssNMR data interpretation.

Conclusions:

  • The described BSH-CP-based 13C-detected ssNMR method is effective for protein backbone and side-chain assignment.
  • This tutorial offers a practical guide for researchers new to ssNMR.
  • The protocol facilitates detailed structural and dynamic studies of proteins under physiological conditions.