Abstract A solid state NMR experiment is introduced for probing relatively slow conformational exchange, based on dephasing and refocusing dipolar couplings. The method is closely related to the previously described Centerband-Only Detection of Exchange or CODEX experiment. The use of dipolar couplings for this application is advantageous because their values are known a priori from molecular structures, and their orientations and reorientations relate in a simple way to molecular geometry and motion. Furthermore the use of dipolar couplings in conjunction with selective isotopic enrichment schemes is consistent with selection for unique sites in complex biopolymers. We used this experiment to probe the correlation time for the motion of 13C, 15N enriched urea molecules within their crystalline lattice.
Content Type Journal Article
Pages 227-232
DOI 10.1007/s10858-009-9353-8
Authors
Wenbo Li, Columbia University Department of Chemistry New York NY 10027 USA
Ann E. McDermott, Columbia University Department of Chemistry New York NY 10027 USA
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Siderocalin Q83 exhibits differential slow dynamics upon ligand binding
Abstract Siderocalin Q83 is a small soluble protein that has the ability to bind two different ligands (enterobactin and arachidonic acid) simultaneously in two distinct binding sites. Here we report that Q83 exhibits an intriguing dynamic behavior. In its free form, the protein undergoes significant micro-to-millisecond dynamics. When binding arachidonic acid, the motions of the arachidonic acid binding site are quenched while the dynamics at the enterobactin binding site increases. Reciprocally, enterobactin...
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09-30-2011 08:01 PM
Cross-Correlations Between Low-? Nuclei in Solids Via a Common Dipolar Bath
Cross-Correlations Between Low-? Nuclei in Solids Via a Common Dipolar Bath
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 July 2011</br>
Aanatoly K., Khitrin , Jiadi, Xu , Ayyalusamy, Ramamoorthy</br>
Correlation of chemical shifts of low-? nuclei (such as 15N) is an important method for assignment of resonances in uniformly-labeled biological solids. Under static experimental conditions, an efficient mixing of low-? nuclear spin magnetization can be achieved by a thermal contact to the common reservoir of...
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07-21-2011 10:31 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] NMR detection of slow conformational dynamics in an endonuclease toxin.
NMR detection of slow conformational dynamics in an endonuclease toxin.
Related Articles NMR detection of slow conformational dynamics in an endonuclease toxin.
J Biomol NMR. 1998 Jul;12(1):145-59
Authors: Whittaker SB, Boetzel R, MacDonald C, Lian LY, Pommer AJ, Reilly A, James R, Kleanthous C, Moore GR
The cytotoxic activity of the secreted bacterial toxin colicin E9 is due to a non-specific DNase housed in the C-terminus of the protein. Double-resonance and triple-resonance NMR studies of the 134-amino acid 15N- and 13C/15N-labelled DNase...
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11-17-2010 11:15 PM
[NMR thesis] Nuclear spin dynamics and thermodynamics of pulsed NMR in solids
Nuclear spin dynamics and thermodynamics of pulsed NMR in solids
Burum, Douglas Peter (1979) Nuclear spin dynamics and thermodynamics of pulsed NMR in solids. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-04302007-153624
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08-27-2010 01:45 AM
[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...
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08-22-2010 03:03 PM
Nitrogen-14 NMR Spectroscopy Using Residual Dipolar Splittings in Solids
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Nitrogen-14 NMR Spectroscopy Using Residual Dipolar Splittings in Solids
Simone Cavadini, Adonis Lupulescu, Sasa Antonijevic,* and Geoffrey Bodenhausen
Laboratoire de Résonance Magnétique Biomoléculaire, Ecole Polytechnique Fédérale de Lausanne, Batochime, CH-1015 Lausanne, Switzerland, and Département de Chimie, associé au CNRS, Ecole Normale Supérieure, 24 rue Lhomond 75231, Paris Cedex 05, France
J. Am. Chem. Soc., 128 (24), 7706 -7707, 2006.
Characterization of slow conformational dynamics in solids: dipolar CODEX
Linear Mode
