Related ArticlesMeasurement of long-range cross-correlation rates using a combination of single- and multiple-quantum NMR spectroscopy in one experiment.
J Am Chem Soc. 2002 Apr 17;124(15):4050-7
Authors: Fruh D, Chiarparin E, Pelupessy P, Bodenhausen G
A method is described to determine long-range cross-correlations between the modulations of an anisotropic chemical shift (e.g., of a C' carbonyl carbon in a protein) and the fluctuations of a weak long-range dipolar interaction (e.g., in cross-correlation between the same C' carbonyl and the H(N) proton of the neighboring amide group). Such long-range correlations are difficult to measure because the corresponding long-range scalar couplings are so small that Redfield's secular approximation is often violated. The method, which combines features of single- and double-quantum NMR spectroscopy, allows one to cancel the effects of dominant short-range dipolar interactions (e.g., between the CSA of the amide nitrogen N and the dipolar coupling to its attached proton H(N)) and is designed so that the secular approximation is rescued even if the scalar coupling between the long-range dipolar coupling partners is very small. The cross-correlation rates thus determined in ubiquitin cover a wide range because of local motions and variations of the CSA tensors.
Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers
Backbone assignment of perdeuterated proteins using long-range H/C-dipolar transfers
Abstract For micro-crystalline proteins, solid-state nuclear magnetic resonance spectroscopy of perdeuterated samples can provide spectra of unprecedented quality. Apart from allowing to detect sparsely introduced protons and thereby increasing the effective resolution for a series of sophisticated techniques, deuteration can provide extraordinary coherence lifetimesâ??obtainable for all involved nuclei virtually without decoupling and enabling the use of scalar magnetization transfers. Unfortunately,...
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NMR Cross-Correlated Relaxation Rates Reveal Ion Coordination Sites in DNA
NMR Cross-Correlated Relaxation Rates Reveal Ion Coordination Sites in DNA
Radovan Fiala, Nad?a S?pac?kova?, Silvie Foldynova?-Tranti?rkova?, Jir?i? S?poner, Vladimi?r Sklena?r? and Luka?s? Tranti?rek
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202397p/aop/images/medium/ja-2011-02397p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202397p
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http://feeds.feedburner.com/~r/acs/jacsat/~4/vJtIag8UbVQ
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08-13-2011 02:47 AM
[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble
Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
J Am Chem Soc. 2005 Jan 19;127(2):476-7
Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM
The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...
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11-24-2010 11:14 PM
[NMR paper] A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY i
A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides.
Related Articles A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides.
J Biomol NMR. 2002 Jul;23(3):181-94
Authors: Feenstra KA, Peter C, Scheek RM, van Gunsteren WF, Mark AE
Three methods for calculating nuclear magnetic resonance cross-relaxation rates from molecular dynamics simulations of small flexible molecules have been compared in terms of their ability to...
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[NMR paper] De novo determination of protein structure by NMR using orientational and long-range
De novo determination of protein structure by NMR using orientational and long-range order restraints.
Related Articles De novo determination of protein structure by NMR using orientational and long-range order restraints.
J Mol Biol. 2000 May 19;298(5):927-36
Authors: Hus JC, Marion D, Blackledge M
Orientational and novel long-range order restraints available from paramagnetic systems have been used to determine the backbone solution structure of the cytochrome c' protein to atomic resolution in the complete absence of restraints derived from...
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11-18-2010 09:15 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
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08-22-2010 03:31 PM
[NMR paper] Defining long range order in NMR structure determination from the dependence of heter
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Related Articles Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy.
Nat Struct Biol. 1997 Jun;4(6):443-9
Authors: Tjandra N, Garrett DS, Gronenborn AM, Bax A, Clore GM
Structure determination by NMR presently relies on short range restraints between atoms in close spatial proximity, principally in the...
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08-22-2010 03:03 PM
Antifreeze Glycoprotein Activity Correlates with Long-Range Protein-Water Dynamics
Antifreeze Glycoprotein Activity Correlates with Long-Range Protein-Water Dynamics
Simon Ebbinghaus et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1051632/aop/images/medium/ja-2010-051632_0004.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society