You are viewing a javascript disabled version of the site. Please enable Javascript for this site to function properly.
Go to headerGo to navigationGo to searchGo to contentsGo to footer
In content section. Select this link to jump to navigation

The evolution of protein NMR

Article type: Review Article

Authors: Campbell, Iain D.;

Affiliations: Department of Biochemistry, University of Oxford, Oxford, UK

Note: [] Address for correspondence: Department of Biochemistry, University of Oxford, South Parks Rd, Oxford OX1 3QU, UK. E-mail: [email protected]

Keywords: Nuclear magnetic resonance, proteins, history, magnets, protein–protein interactions, intrinsically disordered proteins, entropy, structure, dynamics, integrin activation, filamin

DOI: 10.3233/BSI-130055

Journal: Biomedical Spectroscopy and Imaging, vol. 2, no. 4, pp. 245-264, 2013

Published: 2013
Get PDF open access

Abstract

Since the first NMR spectrum of a protein was published over 50 years ago, remarkable technical improvements have led to NMR being recognized as a uniquely powerful tool that can give a wide variety of useful information about macromolecules and their interactions. This article gives an overview of NMR studies of proteins. It presents a personal historical perspective, briefly reviews the current status of the field and reflects on possible future directions. Two specific examples, related to multi-domain complexes and membrane-spanning adhesion receptors, are described to illustrate recent applications. Emphasis is placed on how general advances in molecular biology and technology are changing the nature and focus of NMR studies.

Show more