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2D NMR: Overview of Homonuclear Correlation Techniques

2D NMR: Overview of Homonuclear Correlation Techniques

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.
COSY90 is the standard two-dimensional (2D) COSY experiment that...

Chemical Shift: Internal References and Solvent Effects

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.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...

¹H NMR: Complex Splitting

¹H NMR: Complex Splitting

A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied first.

¹H NMR: Interpreting Distorted and Overlapping Signals

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

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...

2D NMR: Overview of Heteronuclear Correlation Techniques

2D NMR: Overview of Heteronuclear Correlation Techniques

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 axis.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Solid-state NMR-based approaches for supramolecular structure elucidation.

Markus Weingarth¹, Marc Baldus

¹Bijvoet Center for Biomolecular Research, Utrecht University , Padualaan 8, 3584 CH Utrecht, The Netherlands.

Accounts of Chemical Research

|April 17, 2013

Summary

This summary is machine-generated.

Solid-state nuclear magnetic resonance (ssNMR) reveals atomic-level details of supramolecular structures in complex biological systems. This technique dissects intra- and intermolecular interactions, advancing our understanding of biomolecular assemblies.

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Area of Science:

Supramolecular Chemistry
Biophysical Chemistry
Structural Biology

Background:

Supramolecular chemistry studies complexes formed by multiple molecules, stabilized by intermolecular interactions.
These interactions are sensitive to environmental factors like temperature and pressure.
Solid-state nuclear magnetic resonance (ssNMR) provides atomic-scale structural and dynamic information in complex biological systems.

Purpose of the Study:

To discuss how ssNMR can dissect the interplay between intra- and intermolecular interactions.
To describe strategies for tailoring ssNMR methods for supramolecular structure investigation.
To review applications in protein-protein interactions and protein-membrane topology.

Main Methods:

Biochemical and spectroscopic strategies tailored for ssNMR.
Application of ssNMR to study protein-protein interactions and membrane topology.
Integration of ssNMR data with computational and other experimental techniques.

Main Results:

ssNMR enables detailed understanding of supramolecular structure at atomic resolution.
The study reviews recent applications of ssNMR in investigating complex biological systems.
Advancements in ssNMR methodology, including dynamic nuclear polarization, enhance its potential.

Conclusions:

ssNMR is a powerful tool for studying the heterogeneous, dynamic, and transient nature of molecular interactions.
Integration of ssNMR with other methods allows targeting larger and more intricate supramolecular structures.
Future developments in ssNMR and NMR-hybrid strategies will further expand its utility in biological systems.