Related ArticlesSimultaneous processing of solid-state NMR relaxation and 1D-MAS exchange data: the backbone dynamics of free vs. binase-bound barstar.
Biochim Biophys Acta. 2003 Aug 21;1650(1-2):117-27
Authors: Krushelnitsky AG, Hempel G, Reichert D
Two types of dynamic solid-state NMR experiments-relaxation and 1D-MAS exchange-were combined for the investigation of the backbone dynamics of a 15% randomly 15N-enriched protein barstar in both free and binase-bound states. The main novelty of this work is a simultaneous quantitative processing of the results of these two types of experiments that we call Simultaneous Relaxation and Exchange Data Analysis (SREDA) approach. It extends the well-known model-free approach such that it permits to discriminate between various motional models (jumps between different sites, wobbling in a cone, etc.). This objective cannot be achieved by analyzing the relaxation or exchange data separately. The SREDA approach was applied to probe a modification of the average backbone dynamics of barstar upon forming a complex with another protein binase. T(1) and off-resonance T(1rho) relaxation times of 15N backbone nuclei were measured at three temperatures between 0 and 45 degrees C, 1D-MAS exchange (CODEX) data were obtained at room temperature within the mixing time range from 0.3 to 200 ms. It has been found that the barstar backbone participates in two molecular processes with correlation times in the 10(-9)-10(-7) and 10(-3)-10(-2) s ranges. Forming the complex with binase results in a significant decrease of the amplitudes of both motions, suggesting that the complex is a more rigid and stable structure than free barstar.
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Microsecond Time-Scale Conformational Exchange in Proteins: Using Long Molecular Dynamics Trajectory To Simulate NMR Relaxation Dispersion Data
Yi Xue, Joshua M. Ward, Tairan Yuwen, Ivan S. Podkorytov and Nikolai R. Skrynnikov
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206442c/aop/images/medium/ja-2011-06442c_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206442c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/NvRRKHU2H3k
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01-28-2012 05:27 AM
AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra
AssignFit: a program for simultaneous assignment and structure refinement from solid-state NMR spectra
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 8 October 2011</br>
Ye*Tian, Charles D.*Schwieters, Stanley J.*Opella, Francesca M.*Marassi</br>
AssignFit is a computer program developed within the XPLOR-NIH package for the assignment of dipolar coupling (DC) and chemical shift anisotropy (CSA) restraints derived from the solid-state NMR spectra of protein samples with uniaxial order. The method is based on minimizing the difference between...
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10-10-2011 06:27 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
[NMRpipe Yahoo group] TALOS+ for Solid State Data
TALOS+ for Solid State Data
Dear Pipers, Greetings, and Happy 2011 ... Many of you will already be familiar with the TALOS system for predicting protein backbone angles using chemical
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01-05-2011 11:40 PM
[NMR paper] Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Related Articles Improved pulse sequences for pure exchange solid-state NMR spectroscopy.
Magn Reson Chem. 2004 Feb;42(2):285-90
Authors: Vosegaard T, Nielsen NC
Spin-exchange experiments are useful for improving the resolution and establishment of sequential assignments in solid-state NMR spectra of uniformly (15)N-labeled proteins oriented macroscopically in phospholipid bilayers. To exploit this advantage fully, it is crucial that the diagonal peaks in the...
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11-24-2010 09:25 PM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy
Abstract We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual 15Nâ??T 1 timescales). We observed chemical exchange for 6...
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10-27-2010 08:51 AM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
Related Articles Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
J Biomol NMR. 2010 Oct 20;
Authors: Del Amo JM, Fink U, Reif B
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that...
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10-22-2010 06:02 AM
[NMR paper] Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spe
Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy.
J Magn Reson. 1999 Jun;138(2):244-55
Authors: Krushelnitsky A, Reichert D, Hempel G, Fedotov V, Schneider H, Yagodina L, Schulga A
Superslow backbone dynamics of the protein barstar and the polypeptide polyglycine was studied by...