Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure

Overview

Journal Subcell Biochem

Publisher Springer

Specialty Biochemistry

Date 2024 Dec 31

PMID 39738947

Authors

Jose L Neira

Affiliations

Soon will be listed here.

Abstract

Nuclear magnetic resonance (NMR) is a spectroscopic technique based on the absorption of radiofrequency radiation by atomic nuclei in the presence of an external magnetic field. NMR has followed a "bottom-up" approach to solve the structures of isolated domains of viral proteins, including capsid protein subunits, or to provide information about other macromolecular partners with which such proteins interact. NMR has been instrumental in describing conformational changes in viral proteins and nucleic acids, showing the presence of dynamic equilibria which are thought to be important at different stages of the virus life cycle. In this sense, NMR is also the only technique currently available to describe, in atomic detail, the conformational preferences of intrinsically disordered viral proteins. Furthermore, NMR can provide insights into the thermodynamic parameters governing binding reactions between different viral macromolecules. NMR has also complemented X-ray crystallography and has been combined with electron microscopy to obtain pseudo-atomic models of entire virus capsids. Finally, the joint use of liquid and solid-state NMR has allowed the identification of conformational changes in viral capsids upon insertion into host membranes.

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