Nuclear magnetic resonance spectroscopy of proteins is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucl
The NMR sample is prepared in a thin-walled glass tube.
Comparison of a COSY and TOCSY 2D spectra for an amino acid like glutamate or methionine. The TOCSY shows off diagonal crosspeaks between all protons in the spectrum, but the COSY only has crosspeaks between neighbours.
Schematic of an HNCA and HNCOCA for four sequential residues. The nitrogen-15 dimension is perpendicular to the screen. Each window is focused on the nitrogen chemical shift of that amino acid. The sequential assignment is made by matching the alpha carbon chemical shifts. In the HNCA each residue sees the alpha carbon of itself and the preceding residue. The HNCOCA only sees the alpha carbon of the preceding residue.
Nuclear magnetic resonance structure determination generates an ensemble of structures. The structures will converge only if the data is sufficient to dictate a specific fold. In these structures, it is the case for only a part of the structure. From PDB entry 1SSU.
Residual dipolar coupling
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The residual dipolar coupling between two spins in a molecule occurs if the molecules in solution exhibit a partial alignment leading to an incomplete averaging of spatially anisotropic dipolar coupli
Liquid crystals are commonly used to permit the observation of residual dipolar couplings in high-resolution liquid-state NMR spectra.
RDC target curves for the N-H vector of Asp58 in a tight 10-model ensemble for ubiquitin (PDB:1D3Z)