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2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

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Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other...
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2D NMR: Heteronuclear Single-Quantum Correlation Spectroscopy (HSQC)01:19

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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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Structures of Solids02:22

Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Proton (¹H) NMR: Chemical Shift01:07

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Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
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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.
For instance, the proton...
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Inductive Effects on Chemical Shift: Overview01:27

Inductive Effects on Chemical Shift: Overview

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The protons in unsubstituted alkanes are strongly shielded with chemical shifts below 1.8 ppm. Methine, methylene, and methyl protons appear at approximately 1.7, 1.2 and 0.7 ppm, while the proton signal from methane appears at 0.23 ppm. An electronegative substituent, such as chlorine, withdraws the electron density from the protons, increasing their chemical shift. Progressive substitution of the hydrogens in methane by chlorine shifts the proton signals increasingly downfield, to 3.05 ppm in...
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Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins.

W Trent Franks1, Kathryn D Kloepper, Benjamin J Wylie

  • 1Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA.

Journal of Biomolecular NMR
|August 10, 2007
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Summary

New 4D solid-state NMR experiments overcome spectral degeneracy, enabling chemical shift assignment for larger proteins. This advances structure determination for biomolecules previously inaccessible to this technique.

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Area of Science:

  • Biophysical Chemistry
  • Structural Biology
  • Nuclear Magnetic Resonance Spectroscopy

Background:

  • Chemical shift assignment is crucial for protein structure determination using Nuclear Magnetic Resonance (NMR).
  • Magic-angle spinning solid-state NMR (MAS SSNMR) has advanced rapidly, but spectral degeneracy limits its application to larger proteins.
  • Existing 2D and 3D SSNMR correlation experiments struggle with complex spectra of proteins >10 kDa.

Purpose of the Study:

  • To develop and implement 4D backbone chemical shift correlation experiments for unambiguous assignment in solid proteins.
  • To address the challenge of spectral degeneracy in SSNMR of larger proteins.
  • To improve the applicability of SSNMR for structural studies of biomolecules without inherent molecular weight limits.

Main Methods:

  • Implementation of 4D backbone chemical shift correlation experiments.
  • Detailed investigation of the CANCOCX pulse sequence involving multiple cross-polarization steps.
  • Varying homonuclear mixing times to observe short- and long-range correlations.

Main Results:

  • The 4D experiments significantly reduce spectral degeneracy in solid-state NMR spectra.
  • High sensitivity was maintained, consistent with theoretical predictions.
  • A single 4D experiment on the 56-residue protein GB1 revealed over 200 resolved medium- and long-range correlations.
  • Experimental results showed good agreement with theoretical analysis for larger proteins.

Conclusions:

  • 4D backbone correlation experiments are effective for chemical shift assignment in solid proteins, overcoming limitations of previous methods.
  • This technique expands the scope of MAS SSNMR for structural biology, enabling studies of larger and more complex protein systems.
  • The developed methods provide a pathway for more comprehensive structural analysis of proteins in the solid state.