We investigated correlated µs-ms time scale motions of neighboring 13Câ?²â??15N and 13Cαâ??13Cβ nuclei in both protonated and perdeuterated samples of GB3. The techniques employed, NMR relaxation due to cross-correlated chemical shift modulations, specifically target concerted changes in the isotropic chemical shifts of the two nuclei associated with spatial fluctuations. Field-dependence of the relaxation rates permits identification of the parameters defining the chemical exchange rate constant under the assumption of a two-site exchange. The time scale of motions falls into the intermediate to fast regime (with respect to the chemical shift time scale, 100â??400Â*sâ??1 range) for the 13Câ?²â??15N pairs and into the slow to intermediate regime for the 13Cαâ??13Cβ pairs (about 150Â*sâ??1). Comparison of the results obtained for protonated and deuterated GB3 suggests that deuteration has a tendency to reduce these slow scale correlated motions, especially for the 13Cαâ??13Cβ pairs.
[NMR paper] Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.
Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.
Sci Rep. 2017 Aug 07;7(1):7444
Authors: Xue K, Sarkar R, Motz C, Asami S, Camargo DCR, Decker V, Wegner S, Tosner Z, Reif B
Abstract
MAS...
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08-10-2017 12:13 AM
[NMR paper] Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Nonlinear excitations match correlated motions unveiled by NMR in proteins: a new perspective on allosteric cross-talk.
Phys Biol. 2014 Apr 15;11(3):036003
Authors: Piazza F
Abstract
In this paper we propose a novel theoretical framework for interpreting long-range dynamical correlations unveiled in proteins through NMR measurements. The theoretical rationale relies on the hypothesis that correlated...
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04-16-2014 11:07 AM
New amino acid residue type identification experiments valid for protonated and deuterated proteins
New amino acid residue type identification experiments valid for protonated and deuterated proteins
Abstract Two experiments are presented that yield amino acid type identification of individual residues in a protein by editing the 1Hâ??15N correlations into four different 2D subspectra, each corresponding to a different amino acid type class, and that can be applied to deuterated proteins. One experiment provides information on the amino acid type of the residue preceding the detected amide 1Hâ??15N correlation, while the other gives information on the type of its own residue. Versions...
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09-06-2012 05:03 PM
Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems
Radio frequency assisted homonuclear recoupling - A Floquet description of homonuclear recoupling via surrounding heteronuclei in fully protonated to fully deuterated systems
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 18 January 2011</br>
Michal, Leskes , Ümit, Akbey , Hartmut, Oschkinat , Barth-Jan, van Rossum , Shimon, Vega</br>
We present a Floquet theory approach for the analysis of homonuclear recoupling assisted by radio frequency (RF) irradiation of surrounding heteronuclear spins. This description covers a...
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01-19-2011 03:04 PM
[NMR paper] Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.
Biochemistry. 1997 Feb 11;36(6):1389-401
Authors: Gardner KH, Rosen MK, Kay LE
The development of 15N, 13C, 2H multidimensional NMR spectroscopy has facilitated the assignment of backbone and side chain resonances of proteins and protein complexes with molecular masses...
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08-22-2010 03:31 PM
[NMR paper] Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.
Biochemistry. 1997 Feb 11;36(6):1389-401
Authors: Gardner KH, Rosen MK, Kay LE
The development of 15N, 13C, 2H multidimensional NMR spectroscopy has facilitated the assignment of backbone and side chain resonances of proteins and protein complexes with molecular masses...
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08-22-2010 03:03 PM
Help!!Why does a deuterated protein behave even more poorly than the protonated one?
A 20kDa protein, about half of the total signals can be observed in CBCA(CO)NH experiment when protonated with sample concentration of 1mM. However, after deuterated, hardly any signals can be observed with the same concentration in this experiment. We use the same pulse sequence except adding deuterium decoupling in the deuterated one. I don't know why? Help!!
Correlated motions of Câ?²â??N and C α â??C β pairs in protonated and per-deuterated GB3
Linear Mode
