Correlation of proton chemical shifts in proteins using two-dimensional exchange correlated spectroscopy

1984 ◽  
Vol 58 (3) ◽  
pp. 511-516 ◽  
Author(s):  
Jonathan Boyd ◽  
Geoffrey R. Moore ◽  
Glyn Williams
1982 ◽  
Vol 60 (19) ◽  
pp. 2431-2441 ◽  
Author(s):  
Gareth A. Morris ◽  
Laurance D. Hall

Double Fourier transform ("2D") nmr methods allow the simultaneous measurement of proton and carbon-13 chemical shifts for each directly bonded carbon–proton pair in a molecule. As well as greatly increasing the number of different resonances that may be distinguished in the spectra of complex systems, the measurement of correlated proton and carbon-13 shifts allows the otherwise inaccessible proton shifts to be determined, and facilitates the assignment of conventional proton and carbon-13 spectra. Results are presented for glucose, maltose, maltotriose, α-cyclodextrin, β-cyclodextrin, and dextran T-10; reassignments are proposed for the carbon-13 spectra of maltose and maltotriose.


2012 ◽  
Vol 287 (22) ◽  
pp. 18201-18209 ◽  
Author(s):  
Kosuke Ohgo ◽  
Walter P. Niemczura ◽  
Brian C. Seacat ◽  
Steven G. Wise ◽  
Anthony S. Weiss ◽  
...  

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