DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
DEER in Biological Multispin-Systems: A Case Study on the Fatty Acid Binding to Human Serum Albumin
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 10 March 2011</br>
Matthias J.N., Junk , Hans W., Spiess , Dariush, Hinderberger</br>
In this study, self-assembled systems of human serum albumin (HSA) and spin-labeled fatty acids are characterized by double electron–electron resonance (DEER). HSA, being the most important transport protein of the human blood, is capable to host up to seven paramagnetic fatty acid...
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03-11-2011 05:00 PM
The application of micro-coil NMR probe technology to metabolomics of urine and serum
The application of micro-coil NMR probe technology to metabolomics of urine and serum
Abstract Increasing the sensitivity and throughput of NMR-based metabolomics is critical for the continued growth of this field. In this paper the application of micro-coil NMR probe technology was evaluated for this purpose. The most commonly used biofluids in metabolomics are urine and serum. In this study we examine different sample limited conditions and compare the detection sensitivity of the micro-coil with a standard 5 mm NMR probe. Sample concentration is evaluated as a means to leverage the...
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03-09-2011 04:19 AM
[NMR paper] NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural di
NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
Related Articles NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
J Biol Chem. 2005 Jun 17;280(24):22582-9
Authors: Howard MJ, Smales CM
The non-enzymatic reaction between reducing sugars and long-lived proteins in vivo results in the formation of glycation and advanced glycation end products, which alter the properties of proteins including charge,...
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11-25-2010 08:21 PM
[NMR paper] Analysis of competitive binding of ligands to human serum albumin using NMR relaxatio
Analysis of competitive binding of ligands to human serum albumin using NMR relaxation measurements.
Related Articles Analysis of competitive binding of ligands to human serum albumin using NMR relaxation measurements.
J Pharm Biomed Anal. 2004 Feb 4;34(2):247-54
Authors: Cui YF, Bai GY, Li CG, Ye CH, Liu ML
The competitive binding of two ligands, ibuprofen (IBP) and salicylic acid (SAL), to human serum albumin (HSA) was studied by using nuclear magnetic resonance (NMR) relaxation measurements. When the concentration of one ligand was...
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11-24-2010 09:25 PM
[NMR paper] 1H NMR-based determination of the three-dimensional structure of the human plasma fib
1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
Related Articles 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
J Biol Chem. 1993 Apr 25;268(12):8580-9
Authors: Kar L, Lai CS, Wolff CE, Nettesheim D, Sherman S, Johnson ME
Human plasma fibronectin is a plasma glycoprotein that plays an important role in many biological processes. It consists of two...
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08-21-2010 11:53 PM
[NMR paper] 1H NMR spectroscopic studies on the interactions between human plasma antithrombin II
1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Related Articles 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.
Biochemistry. 1992 Mar 3;31(8):2286-94
Authors: Horne A, Gettins P
The effects of length and composition upon the antithrombin-binding properties of heparin have been investigated for two series of structurally related heparin oligosaccharides. Each...
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08-21-2010 11:41 PM
[NMR paper] NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Related Articles NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Free Radic Res Commun. 1990;8(3):175-83
Authors: Barenghi L, Bradamante S, Giudici GA, Vergani C
Human plasma low density lipoprotein has been oxidized at different stages in vitro and analysed by 1H, 13C, and 31P NMR spectroscopy and by biochemical methods. Information was obtained on: a) structure mobilities of lipids and on lipid-protein interactions; b) conjugated and oxo-dienes; c)...
Human serum/plasma lipoprotein analysis by NMR: Application to the study of diabetic dyslipidemia
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