scholarly journals Solid State NMR Strategy for Characterizing Native Membrane Protein Structures

2013 ◽  
Vol 46 (9) ◽  
pp. 2172-2181 ◽  
Author(s):  
Dylan T. Murray ◽  
Nabanita Das ◽  
Timothy A. Cross
Keyword(s):  
Solid State ◽  
Membrane Protein ◽  
Solid State Nmr ◽  
Protein Structures

Protein structure by solid-state NMR spectroscopy

1987 ◽  
Vol 19 (1-2) ◽  
pp. 7-49 ◽  
Author(s):  
S. J. Opella ◽  
P. L. Stewart ◽  
K. G. Valentine
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Information ◽  
Biological Systems ◽  
Genetic Regulation ◽  
Protein Structures ◽  
Crystalline Solid ◽  
Solid State Nmr Spectroscopy ◽  
Nmr Methods

The three-dimensional structures of proteins are among the most valuable contributions of biophysics to the understanding of biological systems (Dickerson & Geis, 1969; Creighton, 1983). Protein structures are utilized in the description and interpretation of a wide variety of biological phenomena, including genetic regulation, enzyme mechanisms, antibody recognition, cellular energetics, and macroscopic mechanical and structural properties of molecular assemblies. Virtually all of the information currently available about the structures of proteins at atomic resolution has been obtained from diffraction studies of single crystals of proteins (Wyckoff et al, 1985). However, recently developed NMR methods are capable of determining the structures of proteins and are now being applied to a variety of systems, including proteins in solution and other non-crystalline environments that are not amenable for X-ray diffraction studies. Solid-state NMR methods are useful for proteins that undergo limited overall reorientation by virtue of their being in the crystalline solid state or integral parts of supramolecular structures that do not reorient rapidly in solution. For reviews of applications of solid-state NMR spectroscopy to biological systems see Torchia and VanderHart (1979), Griffin (1981), Oldfield et al. (1982), Opella (1982), Torchia (1982), Gauesh (1984), Torchia (1984) and Opella (1986). This review describes how solid-state NMR can be used to obtain structural information about proteins. Methods applicable to samples with macroscopic orientation are emphasized.

scholarly journals Solid-State NMR-Restrained Ensemble Dynamics of a Membrane Protein in Explicit Membranes

2015 ◽  
Vol 108 (8) ◽  
pp. 1954-1962 ◽  
Author(s):  
Xi Cheng ◽  
Sunhwan Jo ◽  
Yifei Qi ◽  
Francesca M. Marassi ◽  
Wonpil Im
Keyword(s):  
Solid State ◽  
Membrane Protein ◽  
Solid State Nmr

scholarly journals Exploring Protein Structures by DNP-Enhanced Methyl Solid-State NMR Spectroscopy

2019 ◽  
Vol 141 (50) ◽  
pp. 19888-19901 ◽  
Author(s):  
Jiafei Mao ◽  
Victoria Aladin ◽  
Xinsheng Jin ◽  
Alexander J. Leeder ◽  
Lynda J. Brown ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Protein Structures ◽  
Solid State Nmr Spectroscopy

scholarly journals Resonance assignment of the outer membrane protein AlkL in lipid bilayers by proton-detected solid-state NMR

2020 ◽  
Vol 14 (2) ◽  
pp. 295-300 ◽  
Author(s):  
Tobias Schubeis ◽  
Tom S. Schwarzer ◽  
Tanguy Le Marchand ◽  
Jan Stanek ◽  
Kumar Tekwani Movellan ◽  
...  
Keyword(s):  
Solid State ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Lipid Bilayers ◽  
Resonance Assignment ◽  
Outer Membrane Protein ◽  
Solid State Nmr

scholarly journals Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization

2015 ◽  
Vol 1848 (1) ◽  
pp. 342-349 ◽  
Author(s):  
Kazutoshi Yamamoto ◽  
Marc A. Caporini ◽  
Sang-Choul Im ◽  
Lucy Waskell ◽  
Ayyalusamy Ramamoorthy
Keyword(s):  
Solid State ◽  
Membrane Protein ◽  
Dynamic Nuclear Polarization ◽  
Solid State Nmr ◽  
Nuclear Polarization ◽  
Cellular Solid
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