Related ArticlesNew (15)N NMR exchange experiments for the unambiguous assignment of (1)H(N)/(15)N resonances of proteins in complexes in slow chemical exchange with free form.
J Magn Reson. 2000 Feb;142(2):276-9
Authors: Vialle-Printems C, van Heijenoort C, Guittet E
The potentialities of a 2D proton-detected heteronuclear exchange experiment to assign the nitrogen and amide proton resonances in a uniformly (15)N-enriched macromolecule involved in a complex, starting from the free form assignments, are demonstrated on a protein-DNA complex. This 2D experiment is further extended to a 3D experiment in the case of severe superpositions.
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
AUTOBA: Automation of backbone assignment from HN(C)N suite of experiments
AUTOBA: Automation of backbone assignment from HN(C)N suite of experiments
Abstract Development of efficient strategies and automation represent important milestones of progress in rapid structure determination efforts in proteomics research. In this context, we present here an efficient algorithm named as AUTOBA (Automatic Backbone Assignment) designed to automate the assignment protocol based on HN(C)N suite of experiments. Depending upon the spectral dispersion, the user can record 2D or 3D versions of the experiments for assignment. The algorithm uses as inputs: (i) protein primary...
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06-06-2011 12:53 AM
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Challenges in numerical simulations of solid-state NMR experiments: Spin exchange pulse sequences.
Solid State Nucl Magn Reson. 2011 Feb 1;
Authors: Vosegaard T
While simulations are essential for interpretation of solid-state NMR experiments, large spin systems involved in e.g. spin-diffusion experiments and/or dynamic effects like chemical exchange pose great challenges for the numerical simulations, where we typically want to include effects of...
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02-19-2011 06:02 PM
Corrigendum to “BEST-HNN and 2D (HN)NH experiments for rapid backbone assignment in p
Corrigendum to “BEST-HNN and 2D (HN)NH experiments for rapid backbone assignment in proteins”
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Corrected Proof, Available online 15 September 2010</br>
Dinesh, Kumar , Subhradip, Paul , Ramakrishna V., Hosur</br>
Source: Journal of Magnetic Resonance
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09-16-2010 04:29 PM
[NMR paper] Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of p
Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions.
J Magn Reson. 1999 Feb;136(2):214-8
Authors: Melacini G, Kaptein R, Boelens R
An experimental approach for the editing of exchange-relayed NOEs in water-selective NOE experiments is presented. The...
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08-21-2010 04:03 PM
hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment i
hnCOcaNH and hncoCANH pulse sequences for rapid and unambiguous backbone assignment in (13C, 15N) labeled proteins
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 30 June 2010</br>
Dinesh, Kumar , Jithender G, Reddy , Ramakrishna V., Hosur</br>
Time-saving in data acquisition is a major thrust of NMR pulse sequence development in the context of structural proteomics research. The conventional HNCA and HN(CA)CO pulse sequences, routinely used for sequential backbone assignment, have the limitation that they cannot...
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08-16-2010 03:50 AM
13C-direct detected NMR experiments for the sequential J-based resonance assignment o
Abstract We present here a set of 13C-direct detected NMR experiments to facilitate the resonance assignment of RNA oligonucleotides. Three experiments have been developed: (1) the (H)CC-TOCSY-experiment utilizing a virtual decoupling scheme to assign the intraresidual ribose 13C-spins, (2) the (H)CPC-experiment that correlates each phosphorus with the C4â?˛ nuclei of adjacent nucleotides via J(C,P) couplings and (3) the (H)CPC-CCH-TOCSY-experiment that correlates the phosphorus nuclei with the respective C1â?˛,H1â?˛ ribose signals. The experiments were applied to two RNA hairpin structures....
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08-14-2010 04:19 AM
Suite of Six NMR Relaxation Dispersion Experiments to Study Multiple-Site Exchange in Proteins
http://pubs.acs.org/isubscribe/journals/jacsat/127/i44/figures/ja054550en00001.gif
Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments: An Application to the Folding of a Fyn SH3 Domain Mutant
Dmitry M. Korzhnev, Philipp Neudecker, Anthony Mittermaier, Vladislav Yu. Orekhov, and Lewis E. Kay*
Contribution from the Departments of Medical Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada, and Swedish NMR Center at Göteborg University, Box 465, 405 30 Göteborg, Sweden
J. Am. Chem....