Triple resonance experiments (3D) are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, typically consisting of 1 H, 15 N and 13 C.

Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1 H, 15 N and 13 C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein.

There are a number of important 3D NMR experiments that are used for assigning the peaks in NMR spectra of macromolecules such as proteins, which have been obtained fully labeled with 13 C and 15 N. Additionally, 3D NMR spectroscopy has been used to investigate the structures of synthetic polymers.

'3D NMR Spectra' refers to a type of spectroscopy where a third time axis is introduced, allowing visualization of contour peaks in a cube defined by three axes derived from Fourier transformation steps. It is used for protein structure determination and investigating the structures of macromolecules like proteins and synthetic polymers.

In this Chapter we will show how the well-resolved 2D 15 N-HSQC resonances can be assigned to specific residues and chemical groups within protein samples. As an example, we will consider a couple of complementary types of 3D NMR data: HNCACB and CBCA (CO)NH and their joint application for making heteronuclear NMR resonance assignment in proteins.

HNCA is a 3D triple-resonance NMR experiment commonly used in the field of protein NMR. The name derives from the experiment's magnetization transfer pathway: The magnetization of the amide proton of an amino acid residue is transferred to the amide nitrogen, and then to the alpha carbons of both the starting residue and the previous residue in ...

Feb 2, 2023 · In this comprehensive guide, we will delve deeply into the principles, methodologies, and applications of 2D and 3D NMR spectroscopy, equipping you with a robust understanding of these advanced techniques.

Isotropic mixing The spin-lock reduces the effective chemical shift difference between spins, increasing the efficiency of TOCSY transfer. The magnitude of this effect depends on the strength of the spin-lock relative to the frequency difference: Fundamentals of Protein NMR Spectroscopy, Rule & Hitchens

You have the opportunity to learn and process these 3D data sets with iNMR. The data files have been stripped down, but the “ser” files are intact, so you can open them with other programs like NMRPipe.

3D NMR: Basic Considerations