Author(s)

Shadi Abu-Baker, Gary A. Lorigan

Miami University, Department of Chemistry and Biochemistry, Oxford, USA.

Solid-state NMR spectroscopy is routinely used to determine the structural and dynamic properties of both membrane proteins and peptides in phospholipid bilayers [1-26]. From the perspective of the perpetuated lipids, ²H solid-state NMR spectroscopy can be used to probe the effect of embedded proteins on the order and dynamics of the acyl chains of phospholipid bilayers [8-13]. Moreover, ³¹P solid-state NMR spectroscopy can be used to investigate the interaction of peptides, proteins and drugs with phospholipid head groups [11-14]. The secondary structure of ¹³C = O site-specific isotopically labeled peptides or proteins inserted into lipid bilayers can be probed utilizing 13C CPMAS solid-state NMR spectroscopy [15-18]. Also, solid-state NMR spectroscopic studies can be utilized to ascertain pertinent informa- tion on the backbone and side-chain dynamics of ²H- and ¹⁵N-labeled proteins, respectively, in phospholipid bilayers [19-26]. Finally, specific ¹⁵N-labeled amide sites on a protein embedded inside oriented bilayers can be used to probe the alignment of the helices with respect to the bilayer normal [2]. A brief summary of all these solid-state NMR ap- proaches are provided in this minireview.

Solid-State NMR; Structure and Dynamics; Membrane Proteins

S. Abu-Baker and G. Lorigan, "Solid-State NMR Spectroscopic Approaches to Investigate Dynamics, Secondary Structure and Topology of Membrane Proteins," Open Journal of Biophysics, Vol. 2 No. 4, 2012, pp. 109-116. doi: 10.4236/ojbiphy.2012.24014.