Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in [CH3]-Methyl-Labeled, Deuterated Proteins
Observation and Relaxation Properties of Individual Fast-Relaxing Proton Transitions in -Methyl-Labeled, Deuterated Proteins
Publication year: 2012
Source: Journal of Magnetic Resonance, Available online 2 March 2012</br>
Hechao*Sun, Vitali*Tugarinov</br>
A pair of NMR experiments is developed for separation of individual fast-relaxing transitions inCH3methyl groups of methyl-protonated, highly deuterated proteins, and the measurement of their relaxation rates. Intra-methylH-H/H-C dipole-dipole cross-correlated spin relaxation that differentiates the rates of the fast-relaxing...
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Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins
Abstract Methyl 13CHD2 isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from -glucose/D2O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (Alaβ, Thrγ2) is possible using simple â??out-and-backâ?? NMR methodology. Such selective methyl-detected â??out-and-backâ?? NMR experiments allow complete assignments of threonine γ2...
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[NMR paper] Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
Related Articles Methyl groups as probes for proteins and complexes in in-cell NMR experiments.
J Am Chem Soc. 2004 Jun 9;126(22):7119-25
Authors: Serber Z, Straub W, Corsini L, Nomura AM, Shimba N, Craik CS, Ortiz de Montellano P, Dötsch V
Studying protein components of large intracellular complexes by in-cell NMR has so far been impossible because the backbone resonances are unobservable due to their slow tumbling rates. We describe a methodology that overcomes...
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11-24-2010 09:51 PM
[NMR paper] Selective NMR observation of inhibitor and sugar binding to the galactose-H(+) sympor
Selective NMR observation of inhibitor and sugar binding to the galactose-H(+) symport protein GalP, of Escherichia coli.
Related Articles Selective NMR observation of inhibitor and sugar binding to the galactose-H(+) symport protein GalP, of Escherichia coli.
Biochim Biophys Acta. 2000 Dec 20;1509(1-2):55-64
Authors: Appleyard AN, Herbert RB, Henderson PJ, Watts A, Spooner PJ
The binding of the transport inhibitor forskolin, synthetically labelled with (13)C, to the galactose-H(+) symport protein GalP, overexpressed in its native inner...
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11-19-2010 08:29 PM
[NMR paper] Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
J Biomol NMR. 1997 Apr;9(3):299-305
Authors: Salgado J, Kalverda AP, Canters GW
The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through the...
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08-22-2010 03:31 PM
[NMR paper] Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partia
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
Selective observation of the Cu(I)-amicyanin metal site by paramagnetic NMR on partially oxidised samples.
J Biomol NMR. 1997 Apr;9(3):299-305
Authors: Salgado J, Kalverda AP, Canters GW
The relaxation enhancement caused by paramagnetic copper(II) is used to observe selectivelythe metal site of copper(I)-amicyanin by one- and two-dimensional NMR spectroscopy. Theparamagnetic effect is communicated to the diamagnetic protein through the...
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08-22-2010 03:03 PM
[NMR paper] NMR studies of the methionine methyl groups in calmodulin.
NMR studies of the methionine methyl groups in calmodulin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of the methionine methyl groups in calmodulin.
FEBS Lett. 1995 Jun 12;366(2-3):104-8
Authors: Siivari K, Zhang M, Palmer AG, Vogel HJ
Calmodulin (CaM) is a ubiquitous Ca(2+)-binding protein that can regulate a wide variety of cellular events. The protein contains 9 Met out of a total of 148 amino acid residues. The binding of Ca2+ to CaM induces...
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08-22-2010 03:41 AM
High Resolution 1H Detected 1H,13C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective 1H,2H Isotopic Labeling of Methyl Groups
High Resolution <SUP>1</SUP>H Detected <SUP>1</SUP>H,<SUP>13</SUP>C Correlation Spectra in MAS Solid-State NMR using Deuterated Proteins with Selective <SUP>1</SUP>H,<SUP>2</SUP>H Isotopic Labeling of Methyl Groups
Vipin Agarwal, Anne Diehl, Nikolai Skrynnikov, and Bernd Reif
J. Am. Chem. Soc.; 2006; 128(39) pp 12620 - 12621;
Abstract:
MAS solid-state NMR experiments applied to biological solids are still hampered by low sensitivity and resolution. In this work, we employ a deuteration scheme in which individual methyl groups are selectively protonated. This labeling scheme...
Observation of a Tungsten Alkane ?-Complex Showing Selective Binding of Methyl Groups Using FTIR and NMR Spectroscopies
Linear Mode
