Abstract Reduced dimensionality NMR spectra usually require very large spectral widths in the shared dimension. In this paper we show that aliasing can be introduced in reduced dimensionality NMR spectra either to decrease the acquisition time or increase the resolution of the experiments without losing information. The gains of introducing aliasing are illustrated with two examples, the (3,2)D HNHA and the (4,2)D HN(COCA)NH experiments. In both cases a reduction of the spectral width of more than 50% was possible.
Content Type Journal Article
Pages 351-356
DOI 10.1007/s10858-009-9383-2
Authors
David Pantoja-Uceda, Instituto de QuÃ*mica FÃ*sica Rocasolano, CSIC Serrano 119 28006 Madrid Spain
Jorge Santoro, Instituto de QuÃ*mica FÃ*sica Rocasolano, CSIC Serrano 119 28006 Madrid Spain
Reduced dimensionality 3D HNCANfor unambiguous HN, CA and N assignment in proteins
Reduced dimensionality 3D HNCANfor unambiguous HN, CA and N assignment in proteins
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 8 February 2012</br>
Manoj Kumar*Rout, Pushpa*Mishra, Hanudatta S.*Atreya, Ramakrishna V.*Hosur</br>
We present here an improvisation of HNN (Panchal, Bhavesh et al. 2001)called RD 3D HNCANfor backbone (HN, CA andN) assignment inboth folded and unfolded proteins. This is a reduced dimensionality experiment which employsCAchemical shifts to improve dispersion. Distinct positive and negative peak patternsof various triplet...
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02-10-2012 09:13 AM
[Question from NMRWiki Q&A forum] Folding vs. Aliasing (in NOESY spectra)
Folding vs. Aliasing (in NOESY spectra)
Hi everyone
Does anyone happen to know if/how I can tell whether peaks outside the spectral width were either folded or aliased into a (NOESY) spectrum, when all I have is the spectrum file (in .ucsf format, say), and I do not know how the spectrum was recorded? I am not aiming at finding out whether there were any such 'outside peaks', what I would like to know is, in case there were some, where I would have to look for them.
Thanks a lot for your time!
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02-02-2012 09:43 PM
Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH
Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH
Abstract We present reduced dimensionality (RD) 3D HN(CA)NH for efficient sequential assignment in proteins. The experiment correlates the 15N and 1H chemical shift of a residue (â??iâ??) with those of its immediate N-terminal (i â?? 1) and C-terminal (i + 1) neighbors and provides four-dimensional chemical shift correlations rapidly with high resolution. An assignment strategy is presented which combines the correlations observed in this experiment with amino acid type information obtained from 3D ...
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01-09-2012 08:08 AM
5i. NMR spectroscopy - Examples of NMR spectra
5i. NMR spectroscopy - Examples of NMR spectra
http://i.ytimg.com/vi/2xo0-N0lTl8/default.jpg
5i. NMR spectroscopy - Examples of NMR spectra
Visit www.chemistry.jamesmungall.co.uk for notes on this topic. Thanks for watching! Example of NMR spectra including integration, chemical shift and coupling, and how this correlates with the actual molecular structure. Part of a set of videos giving an introductory course on proton NMR, aimed at around A-level or International Baccalaureate standard. Includes dicussion of integration, chemical shift and coupling.
From:jamesmungall
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06-09-2011 01:40 PM
[NMR paper] Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignm
Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Related Articles Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.
Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):8009-14
Authors: Szyperski T, Yeh DC, Sukumaran DK, Moseley HN, Montelione GT
A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR experiments is presented for rapid and complete protein resonance assignment. Even when using short measurement times, these experiments allow one to retain...
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11-24-2010 08:49 PM
[NMR paper] Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxi
Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin.
FEBS Lett. 1991 Jun 24;284(2):178-83
Authors: Chandrasekhar K, Krause G, Holmgren A, Dyson HJ
As a necessary first step in the use of heteronuclear correlated spectra to obtain high resolution solution structures of the protein, assignment of the...
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08-21-2010 11:16 PM
Nitrogen-detected CAN and CON experiments as alternative experiments for main chain N
Abstract Heteronuclear direct-detection experiments, which utilize the slower relaxation properties of low γ nuclei, such as 13C have recently been proposed for sequence-specific assignment and structural analyses of large, unstructured, and/or paramagnetic proteins. Here we present two novel 15N direct-detection experiments. The CAN experiment sequentially connects amide 15N resonances using 13Cα chemical shift matching, and the CON experiment connects the preceding 13C� nuclei. When starting from the same carbon polarization, the intensities of nitrogen signals detected in the CAN or...
Aliasing in reduced dimensionality NMR spectra: (3,2)D HNHA and (4,2)D HN(COCA)NH experiments as examples
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