Abstract
Nuclear magnetic resonance (NMR) spectroscopy, and particularly solid-state NMR spectroscopy, is a method of choice to study the structure and dynamics of both the lipid and the protein components of model and biological membranes. Different approaches have been developed to study these systems in which the restricted molecular motions result in broad NMR spectra. This contribution will first present an overview of the different techniques used to study lipid bilayers, namely 31p, 2H and 13C solid-state NMR spectroscopy. On the other hand, the study of the structure of membrane peptides and proteins is a rapidly growing field and several methods developed in the last two decades will be presented. These methods allow the investigation of protein systems for which structural information is often difficult to obtain by techniques such as X-ray diffraction and multidimensional solution NMR.
Highlights
During the last two decades, nuclear magnetic resonance (NMR) spectroscopy has become a method of choice for the study of the structure and dynamics of natural and synthetic macromolecules
The introduction of multidimensional NMR techniques has brought a versatile approach to the resolution and assignment of resonances in complex NMR spectra, such as those obtained in proteins [1, 2]
Deuterium, phosphorus and carbon NMR methods have been widely used for the study of the structure and dynamics of biological membranes
Summary
During the last two decades, nuclear magnetic resonance (NMR) spectroscopy has become a method of choice for the study of the structure and dynamics of natural and synthetic macromolecules. The introduction of multidimensional NMR techniques has brought a versatile approach to the resolution and assignment of resonances in complex NMR spectra, such as those obtained in proteins [1, 2] These methods have been used successfully to study small molecules (molecular weight < ∼30,000) in solution. For large proteins, polymers and membrane assemblies, spectral line broadening is encountered due to reduced tumbling rates and correspondingly longer rotational correlation times In such cases, a good alternative is the solid-state NMR technique, which is useful for the study of biological and model membranes [3, 4]. The first section of the paper will be devoted to the study of lipid bilayers by solid-state 31P, 2H and 13C NMR while the second part will present an overview of several techniques to investigate the structure of membrane peptides and proteins
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