Article citationsMore>>

S. Tuzi, A. Naito and H. Saito, “A High-Resolusion Solid-State 13C-NMR Study on [1-13C]Ala and [3-13C] Ala and [1-13C]Leu and Val-Labelled Bacteriorhodopsin: Conformation and Dynamics of Transmembrane Helics, Loops and Termini, and Hydration-Induced Conformational Changes,” European Journal of Biochemistry, Vol. 218, No. 3, 1993, pp. 837-844.

has been cited by the following article:

• TITLE: Solid-State NMR Spectroscopic Approaches to Investigate Dynamics, Secondary Structure and Topology of Membrane Proteins

  AUTHORS: Shadi Abu-Baker, Gary A. Lorigan

  KEYWORDS: Solid-State NMR; Structure and Dynamics; Membrane Proteins

  JOURNAL NAME: Open Journal of Biophysics, Vol.2 No.4, November 1, 2012

  ABSTRACT: 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.