Abstract
Thallapuranam K Suresh Kumar, Ryan Thurman and Srinivas Jayanthi-In-Cell NMR Spectroscopy–<em>In vivo</em> Monitoring of the Structure, Dynamics, Folding, and Interactions of Proteins at Atomic Resolution
Highlights
Multidimensional nuclear magnetic resonance spectroscopy (NMR) is a very versatile technique which is routinely used for the characterization of 3D structure, backbone dynamics, and intermolecular interactions of proteins in solution at atomic resolution
Are the 3D structures of isolated proteins determined under in vitro conditions different than when they are present in a crowded cellular environment with other proteins and biomolecules? Do protein-ligand structural interactions characterized under in vitro conditions bear resemblance to those which occur in the cellular milieu? Most importantly, do post-translational modifications which occur during protein maturation cause significant change in the conformation of proteins? These intriguing questions can be satisfactorily addressed by the recently developed in-cell NMR spectroscopy
Two-dimensional correlation experiments involving NMR sensitive atomic nuclei are primary to the characterization of protein structure and their interactions. 1H-15N/1H-13C HSQC (Heteronuclear Single Quantum Coherence) is the most informative and widely employed 2D correlation experiment used in in-cell NMR spectroscopy. 1H-15N HSQC is preferred over the 1H-13C HSQC experiment due to its simplicity and significantly lower costs of preparation of 15N-enriched protein samples
Summary
In-Cell NMR Spectroscopy-In vivo Monitoring of the Structure, Dynamics, Folding, and Interactions of Proteins at Atomic Multidimensional nuclear magnetic resonance spectroscopy (NMR) is a very versatile technique which is routinely used for the characterization of 3D structure, backbone dynamics, and intermolecular interactions of proteins in solution at atomic resolution. Like X-ray crystallography and electron microscopy, multidimensional NMR spectroscopy has till recently been only conceived as an in vitro technique which can help in the structural characterization of proteins.
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