Solid state nuclear magnetic resonance membrane proteins

Bechinger, B. Zasloff, M. Opella, S.J. "Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy", Protein Sci., 1993,2,2077-2984. 

These semisynthetic proteins have served as useful tools to investigate and study the role of Ras proteins in the cell, for instance, new insights in the so-called Ras acylation cycle could be obtained as well as solid-state nuclear magnetic resonance (NMR) spectroscopic analysis of the lipidated membrane anchor and proteins became possible. ... 

Several interesting review articles have been recently published focusing on the use of NMR methods to study peptide-lipid and small molecular weight molecule interactions in model and natural membranes. Maler as well as Kang and Li highlighted the unique possibilities of solution-state NMR to investigate the structure, dynamics and location of proteins and peptides in artificial bilayers and peptide-lipid interactions. On the other hand, Renault et reviewed recent advances in cellular solid-state nuclear magnetic resonance spectroscopy (SSNMR) to follow the structure, function, and molecular interactions of protein-lipid complexes in their cellular context and at atomic resolution. 

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful method to determine the structure of biomacromolecules and their complexes in solution. It allows determination of the dynamics of proteins, RNA, DNA, and their complexes at atomic resolution. Therefore, NMR spectroscopy can monitor the often transient weak interactions in the interactome of proteins and the interaction between proteins and small-molecule ligands. In addition, intrinsically unstructured proteins can be investigated, and first reports of structure determination of membrane proteins in the immobilized state (solid state) are developing. This review will introduce the fundamental NMR observables as well as the methods to investigate structure and dynamics, and it will discuss several examples where NMR spectroscopy has provided valuable information in the context of Chemical Biology. 

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