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[NMR paper] Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
Related Articles Site-specific 13C chemical shift anisotropy measurements in a uniformly 15N,13C-labeled microcrystalline protein by 3D magic-angle spinning NMR spectroscopy.
J Am Chem Soc. 2005 Aug 31;127(34):11946-7
Authors: Wylie BJ, Franks WT, Graesser DT, Rienstra CM
In this Communication, we introduce a 3D magic-angle spinning recoupling experiment that correlates chemical shift...
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12-01-2010 06:56 PM
[NMR paper] NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evi
NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Related Articles NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Biochemistry. 2005 Feb 22;44(7):2369-77
Authors: Li H, Frieden C
(19)F-Nuclear magnetic resonance (NMR) studies have been carried out after incorporation of 4-(19)F-phenylalanine into the intestinal fatty acid binding protein (IFABP), a...
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11-24-2010 11:14 PM
[NMR paper] Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evi
Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evidence for an unusual peptide bond at the N-extein-intein junction.
Related Articles Semisynthesis of a segmental isotopically labeled protein splicing precursor: NMR evidence for an unusual peptide bond at the N-extein-intein junction.
Proc Natl Acad Sci U S A. 2004 Apr 27;101(17):6397-402
Authors: Romanelli A, Shekhtman A, Cowburn D, Muir TW
Protein splicing is a posttranslational autocatalytic process in which an intervening sequence, termed an intein, is...
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11-24-2010 09:51 PM
[NMR paper] NMR monitoring of accumulation and folding of 15N-labeled protein overexpressed in Pi
NMR monitoring of accumulation and folding of 15N-labeled protein overexpressed in Pichia pastoris.
Related Articles NMR monitoring of accumulation and folding of 15N-labeled protein overexpressed in Pichia pastoris.
Protein Expr Purif. 2001 Jul;22(2):318-24
Authors: de Lamotte F, Boze H, Blanchard C, Klein C, Moulin G, Gautier MF, Delsuc MA
Postgenomic studies have led to an increasing demand for isotope-labeled proteins. We present a method for producing large quantities of truly native (15)N-labeled protein. Based on the secretion...
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11-19-2010 08:44 PM
[NMR paper] Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein r
Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Related Articles Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.
Biochemistry. 2001 Mar 20;40(11):3282-8
Authors: Verhoeven MA, Creemers AF, Bovee-Geurts PH, De Grip WJ, Lugtenburg J, de Groot HJ
...
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11-19-2010 08:32 PM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
J Magn Reson B. 1994 May;104(1):77-80
Authors: Yu L, Meadows RP, Wagner R, Fesik SW
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08-22-2010 03:33 AM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
J Magn Reson B. 1994 May;104(1):77-80
Authors: Yu L, Meadows RP, Wagner R, Fesik SW
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08-22-2010 03:33 AM
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively 13C labeled samples
Patrik Lundström, D. Flemming Hansen and Lewis E. Kay
Journal of Biomolecular NMR; 2008; 42(1); pp 35 - 47
Abstract: Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion nuclear magnetic resonance (NMR) spectroscopy has emerged as a powerful method for quantifying chemical shifts of excited protein states. For many applications of the technique that involve the measurement of relaxation rates of carbon...
of labeled protein for NMR
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