Structure and Dynamics of Membrane Proteins from Solid-State NMR
نویسندگان
چکیده
منابع مشابه
Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy.
The high-resolution structure of membrane proteins is notoriously difficult to determine due to the hydrophobic nature of the protein-membrane complexes. Solid-state NMR spectroscopy is a unique and powerful atomic-resolution probe of the structure and dynamics of these important biological molecules. A number of new solid-state NMR methods for determining the depth of insertion, orientation, o...
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Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the lipid membrane, we have used solid-state NMR spectroscopy to determine the membrane-bound ...
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Solid-state NMR is a versatile and powerful tool for determining the dynamic structure of membrane proteins at atomic resolution. I review the recent progress in determining the orientation, the internal and global protein dynamics, the oligomeric structure, and the ligand-bound structure of membrane proteins with both alpha-helical and beta sheet conformations. Examples are given that illustra...
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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, H 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, P solid...
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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 p...
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ژورنال
عنوان ژورنال: Annual Review of Biophysics
سال: 2018
ISSN: 1936-122X,1936-1238
DOI: 10.1146/annurev-biophys-070816-033712