Related ArticlesHigh-resolution magic angle spinning 1H NMR spectroscopic studies on intact rat renal cortex and medulla.
Magn Reson Med. 1999 Jun;41(6):1108-18
Authors: Garrod S, Humpfer E, Spraul M, Connor SC, Polley S, Connelly J, Lindon JC, Nicholson JK, Holmes E
High-resolution magic angle spinning 1H NMR (MAS-NMR) spectroscopy was used to investigate the biochemical composition of normal renal cortex and renal papilla samples from rats, and results were compared with those from conventional 1H NMR analysis of protein-free tissue extracts. 1H MAS NMR spectra of samples obtained from inner and outer cortex were found to be broadly similar in terms of metabolite profile, and intra- and inter-animal variability was small. However, the MAS NMR spectra from renal papilla samples were qualitatively and quantitatively different from those obtained from cortex. High levels of free amino acids and several organic acids were detected in the cortex, together with choline, glucose, and trimethylamine-N-oxide. The dominant metabolite resonances observed in papillary tissue were from glycerophosphocholine (GPC), betaine, myo-inositol, and sorbitol. On increasing the magic angle spinning rate from 4,200 to 12,000 Hz, the lipid MAS 1H NMR signal profile remained largely unchanged in papillary tissue, whereas "new" resonances from triglycerides appeared in the spectra of cortical tissue, this effect being reversible on returning the spinning rate to 4,200 Hz. Further investigation into the behavior of the lipid components under different spinning rates suggested that the lipids in the cortex were present in more motionally constrained environments than those in the papilla. 1H MAS NMR spectra of tissues are of value both in interrogation of the biochemical composition of whole tissue, and in obtaining information on the mobility and compartmentalization of certain metabolites.
[NMR paper] High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.
High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.
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J Am Chem Soc. 2005 Jul 27;127(29):10138-9
Authors: Sillen A, Wieruszeski JM, Leroy A, Younes AB, Landrieu I, Lippens G
HRMAS NMR of tau paired helical fragments assembled with heparin show an intensity decrease for those amino acids that are incorporated into the rigid core...
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[NMR paper] Magic angle spinning solid-state NMR spectroscopy for structural studies of protein i
Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
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J Am Chem Soc. 2004 Dec 22;126(50):16608-20
Authors: Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V,...
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[NMR paper] Evidence of secondary structure by high-resolution magic angle spinning NMR spectrosc
Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports.
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J Am Chem Soc. 2001 May 9;123(18):4130-8
Authors: Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand JP, Bianco A
The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of...
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[NMR paper] 13C magic angle spinning NMR characterization of the functionally asymmetric QA bindi
13C magic angle spinning NMR characterization of the functionally asymmetric QA binding in Rhodobacter sphaeroides R26 photosynthetic reaction centers using site-specific 13C-labeled ubiquinone-10.
Related Articles 13C magic angle spinning NMR characterization of the functionally asymmetric QA binding in Rhodobacter sphaeroides R26 photosynthetic reaction centers using site-specific 13C-labeled ubiquinone-10.
Biochemistry. 1995 Aug 15;34(32):10229-36
Authors: van Liemt WB, Boender GJ, Gast P, Hoff AJ, Lugtenburg J, de Groot HJ
Photosynthetic...
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[NMR paper] 13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroide
13C magic angle spinning NMR evidence for a 15,15'-cis configuration of the spheroidene in the Rhodobacter sphaeroides photosynthetic reaction center.
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Biochemistry. 1992 Dec 15;31(49):12446-50
Authors: de Groot HJ, Gebhard R, van der Hoef I, Hoff AJ, Lugtenburg J, Violette CA, Frank HA
The photosynthetic reaction center of Rhodobacter sphaeroides 2.4.1 contains one carotenoid...
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[NMR paper] 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of r
13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.
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Biochemistry. 1991 Jul 30;30(30):7409-15
Authors: Smith SO, Courtin J, de Groot H, Gebhard R, Lugtenburg J
Magic-angle spinning NMR spectra have been obtained of the bathorhodopsin photointermediate trapped at low temperature (less than 130 K) by using isorhodopsin samples regenerated with retinal specifically 13C-labeled at positions 8,...
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[NMR paper] 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of r
13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.
Related Articles 13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.
Biochemistry. 1991 Jul 30;30(30):7409-15
Authors: Smith SO, Courtin J, de Groot H, Gebhard R, Lugtenburg J
Magic-angle spinning NMR spectra have been obtained of the bathorhodopsin photointermediate trapped at low temperature (less than 130 K) by using isorhodopsin samples regenerated with retinal specifically 13C-labeled at positions 8,...