Journal
JOURNAL OF MAGNETIC RESONANCE
Volume 204, Issue 1, Pages 160-164Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jmr.2010.02.012
Keywords
Multidimensional NMR; Heteronuclear NMR; HCC(CO)NH-TOCSY; Maximum entropy; Non-uniform sampling; Protein assignment
Funding
- Australian Research Council [DP0774245]
- US National Institutes of Health [GM-47467, RR-020125]
- Queensland Smart State Research Facilities Fund
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One of the stiffest challenges in structural studies of proteins using NMR is the assignment of sidechain resonances. Typically, a panel of lengthy 3D experiments are acquired in order to establish connectivities and resolve ambiguities due to overlap. We demonstrate that these experiments can be replaced by a single 4D experiment that is time-efficient, yields excellent resolution, and captures unique carbon-proton connectivity information. The approach is made practical by the use of non-uniform sampling in the three indirect time dimensions and maximum entropy reconstruction of the corresponding 3D frequency spectrum. This 4D method will facilitate automated resonance assignment procedures and it should be particularly beneficial for increasing throughput in NMR-based structural genomics initiatives. (C) 2010 Elsevier Inc. All rights reserved.
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