Publication year: 2010 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 3 September 2010
S., Jayanthi , N., Sinha , K.V., Ramanathan
Separated Local Field (SLF) spectroscopy is a powerful tool for the determination of structure and dynamics of oriented systems such as membrane proteins oriented in lipid bilayers and liquid crystals. Of many SLF techniques available, Polarization Inversion Spin Exchange at Magic Angle (PISEMA) has found wide application due to its many favorable characteristics. However the pulse sequence suffers from its sensitivity to proton resonance frequency offset. Recently we have proposed a new sequence named 24-SEMA (J. Chem. Phys. 132, 134301, 2010) that overcomes this problem of PISEMA. The present work demonstrates the advantage of 24-SEMA as a highly sensitive SLF...
[NMR paper] TINS, target immobilized NMR screening: an efficient and sensitive method for ligand
TINS, target immobilized NMR screening: an efficient and sensitive method for ligand discovery.
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Chem Biol. 2005 Feb;12(2):207-16
Authors: Vanwetswinkel S, Heetebrij RJ, van Duynhoven J, Hollander JG, Filippov DV, Hajduk PJ, Siegal G
We propose a ligand screening method, called TINS (target immobilized NMR screening), which reduces the amount of target required for the fragment-based approach to drug discovery. Binding is detected by...
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[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
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Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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[NMR paper] Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid
Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid state.
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J Am Chem Soc. 2003 Dec 24;125(51):15831-6
Authors: Paulson EK, Morcombe CR, Gaponenko V, Dancheck B, Byrd RA, Zilm KW
A new indirect detection scheme for obtaining (15)N/(1)H shift correlation spectra in crystalline proteins is described. Excellent water suppression is achieved without the need for pulsed field gradients, and using only a...
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11-24-2010 09:16 PM
[NMR paper] Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mu
Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein.
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Biochemistry. 2002 Oct 8;41(40):11954-62
Authors: Tyler R, Pelczer I, Carey J, Copié V
L75F-TrpR is a temperature-sensitive mutant of the tryptophan repressor protein of Escherichia coli in which surface-exposed residue leucine 75 in the DNA binding domain is replaced with...
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[NMR paper] Convection compensated electrophoretic NMR.
Convection compensated electrophoretic NMR.
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J Magn Reson. 2001 Jun;150(2):126-31
Authors: He Q, Wei Z
A novel method of convection compensated ENMR (CC-ENMR) has been developed to detect electrophoretic motion of ionic species in the presence of bulk solution convection. This was accomplished using a gradient moment nulling technique to remove spectral artifacts from heat-induced convection and using the polarity switch of the applied electric field to retain spin phase modulations...
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11-19-2010 08:32 PM
Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of t
Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein (TrpR): Comparison with the 15N NMR Relaxation Profiles of Wild-Type and A77V Mutant Apo-TrpR Repressors
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Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of t
Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the 15N NMR relaxation profiles of wild type and A77V mutant apo-TrpR repressors.
Related Articles Backbone amide dynamics studies of apo-L75F-TrpR, a temperature sensitive mutant of the tryptophan repressor protein (TrpR): comparison with the 15N NMR relaxation profiles of wild type and A77V mutant apo-TrpR repressors.
Biochemistry. 2010 Aug 18;
Authors: Goel A, Tripet BP, Tyler RC, Nebert LD, Copie V
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