Related ArticlesImproved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Experiment.
Chem Phys Lett. 2010 Jul 9;494(1-3):104-110
Authors: Gopinath T, Veglia G
The atomic structure of small molecules and polypeptides can be attained from anisotropic NMR parameters such as dipolar couplings (DC) and chemical shifts (CS). Separated local field experiments resolve DC and CS correlations into two dimensions. However, crowded NMR spectra represent a significant obstacle for the complete resolution of these anisotropic parameters. Using the PISEMA (Polarization Inversion Spin Exchange at the Magic Angle) experiment as a foundation, we designed new pulse schemes that use a constant time evolution in the dipolar (indirect) dimension to measure DC and CS correlations at high resolution. We demonstrated this approach on a 4-pentyl-4'-cyanobiphenyl (5CB) liquid crystal sample, achieving a resolution enhancement ranging from 30 to 60 % for the resonances in the dipolar dimension. These new experiments open the possibility of obtaining significant resolution enhancement for multidimensional NMR experiments carried out on oriented liquid crystalline samples as well as oriented membrane proteins.
PMID: 20814452 [PubMed - as supplied by publisher]
[NMR paper] Signal identification in NMR spectra with coupled evolution periods.
Signal identification in NMR spectra with coupled evolution periods.
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J Magn Reson. 2005 Sep;176(1):47-53
Authors: Malmodin D, Billeter M
Novel multidimensional NMR experiments rely on modified time-domain sampling schemes to provide significant savings of experimental time. Several approaches are based on the coupling of evolution times resulting in a reduction of the dimensionality of the recorded spectra, and a concomitant saving of experimental time. We...
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We present two new databases of NMR-derived distance and dihedral angle...
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J Magn Reson. 2002 Jun;156(2):181-6
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Multidimensional electrophoretic NMR (ENMR) has been introduced to determine structures of coexisting proteins and protein conformations in solution. Signals of different proteins are separated in a new dimension of electrophoretic flow according to their characteristic electrophoretic mobilities. The electrophoretic interferograms have been generated in the flow...
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein.
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PRODECOMP - program for decomposition of NMR spectra with coupled evolution periods
Multiway Decomposition of NMR Spectra with Coupled Evolution Periods
Daniel Malmodin and Martin Billeter
J. Am. Chem. Soc.; 2005; 127(39), pp 13486 - 13487
http://pubs.acs.org/isubscribe/journals/jacsat/127/i39/figures/ja0545822n00001.gif
Abstract:
Coupling evolution periods in NMR experiments on proteins has recently attracted much attention for its substantial savings in measurement time. Using the concept of multiway decomposition, which already proved useful in many types of NMR applications, the novel tool PRODECOMP decomposes sets of spectra with coupled evolution periods...
Improved Resolution in Dipolar NMR Spectra Using Constant Time Evolution PISEMA Exper
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