Side Chain Resonances in Static Oriented Proton-Decoupled15N Solid-State NMR Spectra of Membrane Proteins

2009 ◽  
Vol 131 (18) ◽  
pp. 6340-6341 ◽  
Author(s):  
Christopher Aisenbrey ◽  
Lydia Prongidi-Fix ◽  
Alexandre Chenal ◽  
Daniel Gillet ◽  
Burkhard Bechinger
1999 ◽  
Vol 576 ◽  
Author(s):  
H. Kimura ◽  
K. Okita ◽  
M. Ichitani ◽  
M. Yonezawa ◽  
T. Sugimoto

ABSTRACTThe thermosetting mechanism of an organosilicon polymer containing carborane has been studied utilizing the 13and 29Si solid-state NMR method. The polymer having C≡C bonds in the main chain and CH═CH2, Si-H bonds, and carborane in the bulky side chain, shows a very highly thermal stability in air by curing. From 13C and 29Si NMR spectra of the polymer, it was found that the intermolecular cross-linking reactions of the polymer was due to (1) the diene reaction between Ph-C≡C and C≡C and (2) the addition reaction between side chain terminal and Ph-C≡C and between CH═CH2 and Si–H, and a very highly thermal stable structure is formed.


1996 ◽  
Vol 86-88 ◽  
pp. 535-538 ◽  
Author(s):  
Masanari Takahashi ◽  
Hiroshi Toyuki ◽  
Masahiro Tatsumisago ◽  
Tsutomu Minami

Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev

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.


1997 ◽  
pp. 255-256 ◽  
Author(s):  
J. F. Green ◽  
K. D. Gwinn ◽  
G. W. Kabalka ◽  
C. L. Anderson

2012 ◽  
Vol 51 (40) ◽  
pp. 9959-9959
Author(s):  
Paul Schanda ◽  
Matthias Huber ◽  
Jérôme Boisbouvier ◽  
Beat H. Meier ◽  
Matthias Ernst

2016 ◽  
Vol 52 (45) ◽  
pp. 7186-7204 ◽  
Author(s):  
Sharon E. Ashbrook ◽  
David McKay

DFT calculations are an important tool in assigning and interpreting NMR spectra of solids: we discuss recent developments and their future potential in the context of NMR crystallography.


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