Accurate measurements of (13)C-(13)C distances in uniformly (13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
Related Articles Accurate measurements of (13)C-(13)C distances in uniformly (13)C-labeled proteins using multi-dimensional four-oscillating field solid-state NMR spectroscopy.
J Chem Phys. 2014 Sep 21;141(11):114201
Authors: Straasų LA, Nielsen JT, Bjerring M, Khaneja N, Nielsen NC
Abstract
Application of sets of (13)C-(13)C 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 (13)C-(13)C distances in uniformly (13)C-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 ((13)C') and aliphatic ((13)Caliphatic) spins with high accuracy. The method is based on an improved version of the four-oscillating field (FOLD) technique [L. A. Straasų, 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 (13)C,(15)N-labeled-L-isoleucine. In a more challenging biological application, FOLD 2D experiments are used to determine a large number of (13)C'-(13)Caliphatic distances in amyloid fibrils formed by the SNNFGAILSS fibrillating core of the human islet amyloid polypeptide with uniform (13)C,(15)N-labeling on the FGAIL fragment.
PMID: 25240350 [PubMed - in process]
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