Publication date: Available online 15 March 2018 Source:Solid State Nuclear Magnetic Resonance
Author(s): Sivakumar Paramsivam, Angela M. Gronenborn, Tatyana Polenova
Chemical shift tensors (CSTs) are an exquisite probe of local geometric and electronic structure. 15N CST are very sensitive to hydrogen bonding, yet they have been reported for very few proteins to date. Here we present experimental results and statistical analysis of backbone amide 15N CSTs for 100 residues of four proteins, two E. coli thioredoxin reassemblies (1-73-(U-13C,15N)/74-108-(U-15N) and 1-73-(U-15N)/74-108-(U-13C,15N)), dynein light chain 8 LC8, and CAP-Gly domain of the mammalian dynactin. The 15N CSTs were measured by a symmetry-based CSA recoupling method, ROCSA. Our results show that the principal component ? 11 is very sensitive to the presence of hydrogen bonding interactions due to its unique orientation in the molecular frame. The downfield chemical shift change of backbone amide nitrogen nuclei with increasing hydrogen bond strength is manifested in the negative correlation of the principal components with hydrogen bond distance for both ?-helical and ?-sheet secondary structure elements. Our findings highlight the potential for the use of 15N CSTs in protein structure refinement. Graphical abstract
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Source:European Journal of Cell Biology, Volume 91, Issue 4</br>
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Structural biology is developing into a universal tool for visualizing biological processes in space and time at atomic resolution. The field has been built by established methodology like X-ray crystallography, electron microscopy and solution NMR and is now incorporating new techniques, such as small-angle X-ray scattering, electron tomography, magic-angle-spinning solid-state...
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3084972/aop/images/medium/ja-2012-084972_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3084972
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Backbone amide 15N chemical shift tensors report on hydrogen bonding interactions in proteins: A magic angle spinning NMR study
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