NMR of Membrane-Associated Peptides and Proteins

Reto Bader, Mirjam Lerch, and Oliver Zerbe 

It is obvious why the spectroscopist wants to investigate the structure of integral membrane proteins or enzymes, whose biological action is linked to the presence of phospholipids such as phospholipase, in a membrane-mimicking environment Why such an environment should also be used for other peptides like hormones becomes more clear when we take into account the membrane compartment theory [10-12] as postulated by R. Schwyzer. This theory states that peptides that target membrane-embedded receptors 

Virus coat HIV gp41 1JAV 19 DPC Membrane-associated helix 113 

Signal sequences PhoE n.a. 21 SDS Helix-break-helix 118 

---

Wang G (2008) NMR of membrane-associated peptides and proteins. Curr Protein Pept Sci 9 50-69... 

NMR of Membrane-Associated Peptides and Proteins 5.3.3.2 Amide H,D Exchange... 

Naito A (2009) Structure elucidation of membrane-associated peptides and proteins in oriented bilayers by solid-state NMR spectroscopy. Solid State Nucl Mag 36 67-76... 

The generally low sensitivity of solid state NMR is significantly enhanced by using selective F-labels to analyze the structures of membrane-associated peptides and proteins [13,16-24]. This opens up a previously inaccessible range of experimental conditions, such as peptideiHpid ratios as low as 1 3000 [2 5 ]. This is particularly relevant for antibiotic peptides, as their concentration dependence constitutes an essential functional aspect [26]. A suitable side chain for labelling is 4F-phenylglycine (4F-Phg), as the F-reporter is fixed... 

Membranes and model membranes exhibit liquid crystalline behavior and this has been exploited in a number of studies to obtain valuable information on the structure and dynamics of membrane associated peptides and proteins as well as on the interaction of the peptides with the membranes themselves. NMR spectroscopy of nuclei such as proton, carbon, deuterium, nitrogen and phosphorus has been utilized for such purposes. Structure elucidation of membrane-associated peptides and proteins in oriented bilayers by solid-state NMR spectroscopy has been reviewed. A survey on the use of static uniaxially oriented samples for structural and topological analysis of membrane-associated polypeptides is available. The theoretical background has been dealt with and a number of examples of applications provided. In addition, ongoing developments combining this method with information from solution NMR spectroscopy and molecular modelling as well as exploratory studies using dynamic nuclear polarization solid-state NMR have been presented. The use of N chemical shift anisotropy, dipolar interactions and the deuterium quadrupolar split-... 

The magnetic alignment and liquid crystalline behaviour exhibited by membranes and model membranes have been exploited in a number of studies to obtain valuable information on the structure and dynamics of membrane associated peptides and proteins as well as on the perturbation caused on the membranes themselves by the presence of the probe molecules. NMR spectroscopy of nuclei such as proton, carbon, deuterium, nitrogen and phosphorus has been exploited for this purpose. Several experiments designed to extract information on the peptide structure and... 

Dynamic Aspects of Membrane Proteins and Membrane-Associated Peptides as Revealed by 13C NMR Lessons from Bacteriorhodopsin as an Intact Protein... 

Volume 47 of Annual Reports on NMR contains egregious accounts of modem applications of NMR spectroscopy in four distinct areas of scientific research. It is my very pleasant responsibility to thank all of the contributors to this volume for their considerable efforts in the production of their timely accounts. The first chapter covers progress in the Application of 207Pb NMR Parameters by B. Wrackmeyer, providing an update on this area of activity which was previously reviewed in volume 22 of this series. Following this, H. Saito, S. Tuzi, M. Tanio and A. Naito review Dynamic Aspects of Membrane Proteins and Membrane-Associated Peptides as Revealed by 13C NMR Lessons from Bacteriorhodopsin as an Intact Protein. Applications of NMR to Food Science is an area of activity last visited in volume 32 of this series, and more recent developments are discussed by E. Alberti, P. S. Belton and A. M. Gil in the third chapter. The final contribution by K. K. Laali and T. Okazaki is on NMR of Persistent Carbocations from Polycyclic Aromatic Hydrocarbons. 

---