Abstract A TROSY-selected ZZ-exchange experiment is described for measuring slow chemical exchange rates by monitoring the TROSY component of 15N longitudinal magnetization. Application of the proposed pulse sequence to the cadherin 8 N-terminal extracelluar domain demonstrates that enhanced sensitivity is obtained, compared to a previously described TROSY-detected ZZ-exchange sequence (Sahu et al. J Am Chem Soc 129: 13232â??13237, 2007), by preserving the TROSY effect during the mixing period as well as the frequency encoding periods.
Content Type Journal Article
Pages 357-360
DOI 10.1007/s10858-009-9385-0
Authors
Ying Li, Columbia University Department of Biochemistry and Molecular Biophysics 630 West 168th Street New York NY 10032 USA
Arthur G. Palmer, Columbia University Department of Biochemistry and Molecular Biophysics 630 West 168th Street New York NY 10032 USA
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins
Abstract Multiplet-filtered and gradient-selected heteronuclear zero-quantum coherence (gsHZQC) TROSY experiments are described for measuring 1Hâ??13C correlations for 13CH3 methyl groups in proteins. These experiments provide improved suppression of undesirable, broad outer components of the heteronuclear zero-quantum multiplet in medium-sized proteins, or in flexible sites of larger proteins, compared to previously described HZQC sequences (Tugarinov et al. in J Am Chem Soc...
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Measuring Screw-Sense Preference in a Helical Oligomer by Comparison of 13C NMR Signal Separation at Slow and Fast Exchange
Measuring Screw-Sense Preference in a Helical Oligomer by Comparison of 13C NMR Signal Separation at Slow and Fast Exchange
Jordi Sola?, Gareth A. Morris and Jonathan Clayden
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1097034/aop/images/medium/ja-2010-097034_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1097034
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/NJjFWlcOo9Q
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Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Very simple combination of TROSY, CRINEPT and multiple quantum coherence for signal enhancement in an HN(CO)CA experiment for large proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 February 2011</br>
Monika, Bayrhuber , Roland, Riek</br>
Sensitivity enhancement in liquid state nuclear magnetic resonance (NMR) triple resonance experiments for the sequential assignment of proteins is important for the investigation of large proteins or protein complexes. We present here the 3D TROSY-MQ/CRINEPT-HN(CO)CA which makes...
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[NMR paper] Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid s
Observation of slow dynamic exchange processes in Ras protein crystals by 31P solid state NMR spectroscopy.
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Authors: Stumber M, Geyer M, Graf R, Kalbitzer HR, Scheffzek K, Haeberlen U
The folding, structure and biological function of many proteins are inherently dynamic properties of the protein molecule. Often, the respective molecular processes are preserved upon protein...
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[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.
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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.
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15NH/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: a
Abstract Amide solvent exchange rates are regarded as a valuable source of information on structure/dynamics of unfolded (disordered) proteins. Proton-based saturation transfer experiments, normally used to measure solvent exchange, are known to meet some serious difficulties. The problems mainly arise from the need to (1) manipulate water magnetization and (2) discriminate between multiple magnetization transfer pathways that occur within the proton pool. Some of these issues are specific to unfolded proteins. For example, the compensation scheme used to cancel the Overhauser effect in the...
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins
Linear Mode
