Related ArticlesUsing Paramagnetism to Slow Down Nuclear Relaxation in Protein NMR.
J Phys Chem Lett. 2016 Dec 01;7(23):4815-4818
Authors: Orton HW, Kuprov I, Loh CT, Otting G
Abstract
Paramagnetic metal ions accelerate nuclear spin relaxation; this effect is widely used for distance measurement and called paramagnetic relaxation enhancement (PRE). Theoretical predictions established that, under special circumstances, it is also possible to achieve a reduction in nuclear relaxation rates (negative PRE). This situation would occur if the mechanism of nuclear relaxation in the diamagnetic state is counterbalanced by a paramagnetic relaxation mechanism caused by the metal ion. Here we report the first experimental evidence for such a cross-correlation effect. Using a uniformly (15)N-labeled mutant of calbindin D9k loaded with either Tm(3+) or Tb(3+), reduced R1 and R2 relaxation rates of backbone (15)N spins were observed compared with the diamagnetic reference (the same protein loaded with Y(3+)). The effect arises from the compensation of the chemical shift anisotropy tensor by the anisotropic dipolar shielding generated by the unpaired electron spin.
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
J Magn Reson. 2014 Sep 20;248C:8-12
Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K
Abstract
(15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms...
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10-06-2014 12:37 PM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy
Abstract We developed a new method to elucidate the binding kinetics kon and koff, and the dissociation constant KD (=koff/kon), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular weight in a complex with a large target protein. In our method, kon and koff rates are calculated from the analysis of longitudinal relaxation rates of free resonances measured for multiple samples containing different...
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06-06-2011 12:53 AM
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.
J Biomol NMR. 2011 May 28;
Authors: Sugase K
We developed a new method to elucidate the binding kinetics k(on) and k(off), and the dissociation constant K(D) (=k(off)/k(on)), of protein-protein interactions without observable bound resonances of the protein of interest due to high molecular...
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06-01-2011 02:30 PM
[NMR paper] Strategy for the study of paramagnetic proteins with slow electronic relaxation rates
Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by nmr spectroscopy: application to oxidized human ferredoxin.
Related Articles Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by nmr spectroscopy: application to oxidized human ferredoxin.
J Am Chem Soc. 2004 May 5;126(17):5413-26
Authors: Machonkin TE, Westler WM, Markley JL
NMR studies of paramagnetic proteins are hampered by the rapid relaxation of nuclei near the paramagnetic center, which prevents the application...
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11-24-2010 09:51 PM
[NMR paper] Slow internal dynamics in proteins: application of NMR relaxation dispersion spectros
Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme.
Related Articles Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme.
J Am Chem Soc. 2002 Feb 20;124(7):1443-51
Authors: Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE
Recently developed carbon transverse relaxation dispersion experiments (Skrynnikov, N. R.; et al. J. Am. Chem. Soc. 2001, 123, 4556-4566) were...
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11-24-2010 08:49 PM
[NMR paper] Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Related Articles Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
J Am Chem Soc. 2001 May 2;123(17):3953-9
Authors: Baber JL, Szabo A, Tjandra N
The interpretation of NMR relaxation data for macromolecules possessing slow interdomain motions is considered. It is shown how the "extended model-free approach" can be used to analyze (15)N backbone relaxation data acquired at three different field strengths for Xenopus Ca(2+)-ligated...
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11-19-2010 08:32 PM
[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...
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08-22-2010 03:31 PM
[NMR paper] NMR 15N relaxation and structural studies reveal slow conformational exchange in bars
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
J Mol Biol. 1997 May 2;268(2):494-511
Authors: Wong KB, Fersht AR, Freund SM
Barstar an 89-residue protein consisting of four helices and a three-stranded parallel beta-sheet, is the intracellular inhibitor of the...