scholarly journals 2P042 Structural analysis of amyloid fibril formed in human calcitonin peptide DFNKF as revealed by ^C solid-state NMR spectroscopy

2005 ◽  
Vol 45 (supplement) ◽  
pp. S130
Author(s):  
K. Daidoji ◽  
H. Fujita ◽  
R. Inoue ◽  
K. Nishimura ◽  
A. Naito
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Solid State Nmr ◽  
Amyloid Fibril ◽  
Human Calcitonin ◽  
Solid State Nmr Spectroscopy

Surface structural analysis of selectively 13C-labeled cellulose II by solid-state NMR spectroscopy

Cellulose ◽  
2019 ◽  
Vol 27 (4) ◽  
pp. 1899-1907 ◽  
Author(s):  
Yusuke Kita ◽  
Ryosuke Kusumi ◽  
Tsunehisa Kimura ◽  
Motomitsu Kitaoka ◽  
Yusuke Nishiyama ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Solid State Nmr ◽  
Cellulose Ii ◽  
Solid State Nmr Spectroscopy

scholarly journals Rapid structural analysis of minute quantities of organic solids by exhausting 1H polarization in solid-state NMR spectroscopy at fast MAS

2021 ◽  
Author(s):  
Zhiwei Yan ◽  
Rongchun Zhang
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Chemical Shift ◽  
Solid State Nmr ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Organic Solids ◽  
Solid State Nmr Spectroscopy ◽  
Experimental Time

Solid-state nuclear magnetic resonance (NMR) is a powerful and indispensable tool for structural and dynamic studies of various challenging systems. Nevertheless, it often suffers from significant limitations due to the inherent low signal sensitivity when low- nuclei are involved. Herein, we report an efficient solid-state NMR approach for rapid and efficient structural analysis of minute amounts of organic solids. By encoding staggered chemical shift evolution in the indirect dimension and staggered acquisition in 1H dimension, a proton-detected homonuclear 1H/1H and heteronuclear 13C/1H chemical shift correlation (HETCOR) spectrum can be obtained simultaneously in a single experiment at fast magic-angle-spinning (MAS) conditions with barely increasing experimental time, compared to conventional proton-detected HETCOR experiment. We establish that abundant 1H polarization can be efficiently manipulated and fully utilized in proton-detected solid-state NMR spectroscopy for extraction of more critical structural information and thus reduction of total experimental time.

ChemInform Abstract: Peptide Structural Analysis by Solid-State NMR Spectroscopy

ChemInform ◽  
2010 ◽  
Vol 31 (9) ◽  
pp. no-no
Author(s):  
Burkhard Bechinger ◽  
Rudolf Kinder ◽  
Michael Helmle ◽  
Titus C. B. Vogt ◽  
Ulrike Harzer ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy

Peptide structural analysis by solid-state NMR spectroscopy

Biopolymers ◽  
1999 ◽  
Vol 51 (3) ◽  
pp. 174-190 ◽  
Author(s):  
Burkhard Bechinger ◽  
Rudolf Kinder ◽  
Michael Helmle ◽  
Titus C. B. Vogt ◽  
Ulrike Harzer ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy
Sign in / Sign up

Export Citation Format

Share Document