Abstract
Solvent ordering at an interface can be studied by multiple-quantum NMR. Quantitative studies of (2)H2O ordering require clean double-quantum (2Q) filtration and an analysis of 2Q buildup curves that accounts for relaxation and, if randomly oriented samples are used, the distribution of residual couplings. A pulse sequence with absorption mode detection is extended for separating coherences by order and measuring relaxation times such as the 2Q filtered T2. Coherence separation is used to verify 2Q filtration and the 2Q filtered T2 is required to extract the coupling from the 2Q buildup curve when it is unresolved. With our analysis, the coupling extracted from the buildup curve in (2)H2O hydrated collagen was equivalent to the resolved coupling measured in the usual 1D experiment and the 2Q to 1Q signal ratio was in accord with theory. Application to buildup curves from (2)H2O hydrated elastin, which has an unresolved coupling, revealed a large increase in the 2Q signal upon mechanical stretch that is due to an increase in the ordered water fraction while changes in the residual coupling and T2 are small.
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04-06-2014 02:46 PM
[Question from NMRWiki Q&A forum] Varian FIDs ordering: Inner and outer loop in the sequence(Rance-Kay & States)?
Varian FIDs ordering: Inner and outer loop in the sequence(Rance-Kay & States)?
Dear all,
I am new to NMR and I have difficulty understanding the ordering of FIDs, e.g. if an experiment uses both Rance-Kay and States, there will be loops(outer/inner) which need to be taken care during data processing. I don't completely understand how FIDs(indirect dimension) are stored and in what order. In a pulse sequnece, what an inner or outer loop corresponds to?
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03-24-2013 10:59 PM
[NMR paper] Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Jan 18;
Authors: Asami S, Rakwalska-Bange M, Carlomagno T, Reif B
Abstract
Both protonated and deuterated samples were employed in the study of the L7Ae box C/D RNA complex by (1) H-detected...
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[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
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J Am Chem Soc. 2005 Apr 27;127(16):5826-32
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Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
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11-25-2010 08:21 PM
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Methods Mol Biol. 2004;278:123-38
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The combination of chemical shift, residual dipolar coupling, and backbone relaxation data can be used to characterize the nature of a domain interface in a multidomain protein. Comparison of the parameters obtained from isolated domains and domain pairs provides insight into the composition of the interface as well as into interdomain dynamics. The interface between...
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[NMR paper] Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the
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J Biomol NMR. 1998 Jul;12(1):51-71
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We report the NMR resonance assignments for a macromolecular...
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[NMR paper] A 1H NMR comparative study of the structure of the critical packing interfaces betwee
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 1H NMR comparative study of the structure of the critical packing interfaces between helix and non-helical region in various ligation states of sperm whale myoglobin.
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Structural determination of biomolecular interfaces by nuclear magnetic resonance of
Abstract Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation. Although powerful, these techniques cannot provide unambiguous estimates of intermolecular distances between interacting proteins. Here, we present an alternative approach, called REDSPRINT (REDduced/Standard PRoton density INTerface identification), to map protein interfaces with...
2Q NMR of (2)H2O ordering at solid interfaces.
Linear Mode
