Related Articles1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse lens.
Biochim Biophys Acta. 2000 Mar 6;1474(1):23-30
Authors: Nakamura K, Jung YM, Era S, Sogami M, Ozaki Y, Takasaki A
In order to provide new insight into the molecular mechanism of perforating trauma-induced cataract formation in an 8-week-old ddY mouse lens, we performed an in situ investigation into changes in the water-protein and/or protein-protein interactions by using 500 MHz (1)H-NMR spectroscopy, and into structural alterations in lens proteins by using Raman spectroscopy. Cross-relaxation times of water protons in the perforated opaque lens were considerably shorter than those in the intact transparent lens, whereas there was no significant difference in water content, suggesting a drastic change in water-protein and protein-protein interactions in the perforated lens. In addition, there was no significant difference in the intensity ratios of several key Raman bands between intact and perforated lenses, indicating that no significant local and overall conformational changes in lens protein itself occur in the perforated lens. The present (1)H-NMR and Raman results lead us to the conclusion that changes leading to lens opacification in the perforating trauma-induced cataract appear to involve the rapid formation of immobile large lens protein aggregates without formation of intra- and intermolecular disulfide linkages, and rapid increase in a fraction of bound water associated with large protein aggregates.
[NMR paper] Proton NMR spectroscopy shows lipids accumulate in skeletal muscle in response to burn trauma-induced apoptosis.
Proton NMR spectroscopy shows lipids accumulate in skeletal muscle in response to burn trauma-induced apoptosis.
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FASEB J. 2005 Sep;19(11):1431-40
Authors: Astrakas LG, Goljer I, Yasuhara S, Padfield KE, Zhang Q, Gopalan S, Mindrinos MN, Dai G, Yu YM, Martyn JA, Tompkins RG, Rahme LG, Tzika AA
Burn trauma triggers hypermetabolism and muscle wasting via increased cellular protein degradation and apoptosis. Proton...
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[NMR paper] Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. str
Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. strain CBS3 4-hydroxybenzoyl-CoA thioesterase active site.
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Biochemistry. 2002 Sep 17;41(37):11152-60
Authors: Zhuang Z, Song F, Zhang W, Taylor K, Archambault A, Dunaway-Mariano D, Dong J, Carey PR
4-Hydroxybenzoyl-coenzyme A (4-HBA-CoA) thioesterase catalyzes the hydrolysis of 4-HBA-CoA to 4-hydroxybenzoate...
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[NMR paper] NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric h
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FEBS Lett. 2002 Mar 27;515(1-3):165-70
Authors: Chang X, Keller D, O'Donoghue SI, Led JJ
Nuclear magnetic resonance (NMR) spectroscopy reveals that higher-order aggregates of glucagon-like peptide-1-(7-36)-amide (GLP-1) in pure water at pH 2.5 are disrupted by 35% 2,2,2-trifluoroethanol (TFE), and form a stable and highly symmetric...
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[NMR paper] NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(I
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Biochim Biophys Acta. 1998 Jun 11;1385(1):7-16
Authors: Aime S, Bettinelli M, Ferrari M, Razzano E, Terreno E
At physiological pH and in the presence of an excess of malonate ligand (MAL), the lanthanide ions (Ln=Eu(III), Gd(III) and Tb(III)) are under the form of -. Upon addition of human serum albumin (HSA),...
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[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
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Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
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[NMR paper] Effect of disulfide bridge formation on the NMR spectrum of a protein: studies on oxi
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J Biomol NMR. 1994 May;4(3):411-32
Authors: Chandrasekhar K, Campbell AP, Jeng MF, Holmgren A, Dyson HJ
As a prelude to complete structure calculations of both the oxidized and reduced forms of Escherichia coli thioredoxin (M(r) 11,700), we have analyzed the NMR...
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[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
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Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
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08-22-2010 03:33 AM
[NMR paper] 1H and 31P NMR and HPLC studies of mouse L1210 leukemia cell extracts: the effect of
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Magn Reson Med. 1991 Mar;18(1):142-58
Authors: Berners-Price SJ, Sant ME, Christopherson RI, Kuchel PW
The effect of the antitumor complex Cl (where dppe is Ph2P(CH2)2PPh2) on the overall metabolism of cultured mouse L1210 leukemia cells...
1H-NMR and raman studies on perforating trauma-induced cataract formation in a mouse
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