Related ArticlesRemodeling of HDL by phospholipid transfer protein: demonstration of particle fusion by 1H NMR spectroscopy.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):910-6
Authors: Korhonen A, Jauhiainen M, Ehnholm C, Kovanen PT, Ala-Korpela M
There is evidence that phospholipid transfer protein (PLTP) can increase reverse cholesterol transport by inducing favorable subclass distribution in the high density lipoprotein (HDL) fraction. This includes generation of initial cholesterol acceptor particles, pre beta-HDL, and of enlarged particles that are rapidly cleared from the circulation. However, partly because of methodological difficulties, the mechanisms behind the PLTP-mediated interconversion of HDL particles are not fully understood. In this communication, we describe the use of a novel methodology, based on 1H NMR spectroscopy, to study the PLTP-induced size changes in the HDL particles. In accordance with native gradient gel electrophoresis, the 1H NMR data revealed a gradual production of enlarged HDL particles in the HDL3+ PLTP mixtures. In addition, according to a physical model for lipoprotein particles, relating the frequency shifts observable with NMR to the size of the lipoprotein particles, the NMR data demonstrated that PLTP-mediated HDL remodeling involves fusion of the HDL particles.
[NMR paper] An efficient fusion expression system for protein and peptide overexpression in Esche
An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Related Articles An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Protein Pept Lett. 2003 Apr;10(2):175-81
Authors: Cheng Y, Liu D, Feng Y, Jing G
An efficient fusion expression system with a small fusion partner, His6-tagged N-terminal fragment of staphylococcal nuclease R, has been constructed and tested with two genes. The results show that...
[NMR paper] Demonstration of protein-protein interaction specificity by NMR chemical shift mappin
Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.
Protein Sci. 1997 Dec;6(12):2624-7
Authors: Rajagopal P, Waygood EB, Reizer J, Saier MH, Klevit RE
...
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[NMR paper] Demonstration of positionally disordered water within a protein hydrophobic cavity by
Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Related Articles Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.
Science. 1995 Mar 24;267(5205):1813-7
Authors: Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM
The presence and location of water of hydration (that is, bound water) in the solution structure of human interleukin-1 beta (hIL-1 beta) was investigated with water-selective two-dimensional heteronuclear magnetic resonance spectroscopy. It is shown...
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[NMR paper] Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: s
Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Related Articles Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Biochemistry. 1991 Dec 10;30(49):11600-8
Authors: Simorre JP, Caille A, Marion D, Marion D, Ptak M
Two- and three-dimensional 1H NMR experiments have been used to sequentially assign nearly all proton resonances of the 90 residues of wheat...
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[NMR paper] Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: s
Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Related Articles Two- and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure.
Biochemistry. 1991 Dec 10;30(49):11600-8
Authors: Simorre JP, Caille A, Marion D, Marion D, Ptak M
Two- and three-dimensional 1H NMR experiments have been used to sequentially assign nearly all proton resonances of the 90 residues of wheat...