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Accurate measurements of 13C-13C distances in uniformly 13C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
- Source :
-
Journal of Chemical Physics . 9/21/2014, Vol. 141 Issue 11, p1-12. 12p. 1 Diagram, 4 Charts, 3 Graphs. - Publication Year :
- 2014
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Abstract
- Application of sets of 13C-13C internuclear distance restraints constitutes a typical key element in determining the structure of peptides and proteins by magic-angle-spinning solid-state NMR spectroscopy. Accurate measurements of the structurally highly important 13C-13C distances in uniformly 13C-labeled peptides and proteins, however, pose a big challenge due to the problem of dipolar truncation. Here, we present novel two-dimensional (2D) solid-state NMR experiments capable of extracting distances between carbonyl (13C′) and aliphatic (13Caliphatic) spins with high accuracy. The method is based on an improved version of the four-oscillating field (FOLD) technique [L. A. Straasø, M. Bjerring, N. Khaneja, and N. C. Nielsen, J. Chem. Phys.130, 225103 (2009)] which circumvents the problem of dipolar truncation, thereby offering a base for accurate extraction of internuclear distances in many-spin systems. The ability to extract reliable accurate distances is demonstrated using one- and two-dimensional variants of the FOLD experiment on uniformly 13C,15N-labeled-L-isoleucine. In a more challenging biological application, FOLD 2D experiments are used to determine a large number of 13C′-13Caliphatic distances in amyloid fibrils formed by the SNNFGAILSS fibrillating core of the human islet amyloid polypeptide with uniform 13C,15N-labeling on the FGAIL fragment. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ACCURACY
*UNIFORMITY
*PROTEINS
*ISOLEUCINE
*POLYPEPTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 00219606
- Volume :
- 141
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Journal of Chemical Physics
- Publication Type :
- Academic Journal
- Accession number :
- 98485159
- Full Text :
- https://doi.org/10.1063/1.4895527