ChemInform Abstract: Advanced Solid-State NMR Methods for the Elucidation of Structure and Dynamics of Molecular, Macromolecular, and Supramolecular Systems

ChemInform ◽  
2010 ◽  
Vol 33 (15) ◽  
pp. no-no
Author(s):  
Steven P. Brown ◽  
Hans Wolfgang Spiess
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Supramolecular Systems ◽  
Structure And Dynamics ◽  
Nmr Methods

scholarly journals Structure and dynamics from solid-state NMR spectroscopy

Structure ◽  
1994 ◽  
Vol 2 (8) ◽  
pp. 699-701 ◽  
Author(s):  
RR Ketchem ◽  
W Hu ◽  
F Tian ◽  
TA Cross
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy ◽  
Structure And Dynamics

Structure and Dynamics of LiPON and NaPON Oxynitride Phosphate Glasses by Solid-State NMR

2021 ◽  
Vol 125 (7) ◽  
pp. 4077-4085
Author(s):  
Francisco Muñoz ◽  
Jinjun Ren ◽  
Leo van Wüllen ◽  
Tongyao Zhao ◽  
Holger Kirchhain ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Phosphate Glasses ◽  
Structure And Dynamics

Solid state NMR of membrane proteins: methods and applications

2021 ◽  
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Lipid Membrane ◽  
Cell Function ◽  
Membrane Lipid ◽  
Pharmacological Intervention ◽  
Nmr Methods ◽  
Informative Approach

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

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.

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