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Your search keyword '"Segelke, Brent W."' showing total 3 results
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3 results on '"Segelke, Brent W."'

1. Interaction of the N-terminal domain of apolipoprotein E4 with heparin

Author

Dong, Jun, Peters-Libeu, Clare A., Weisgraber, Karl H., Segelke, Brent W., Rupp, Bernhard, Capila, Ishan, Hernaiz, Maria J., LeBrun, Laurie A., and Linhardt, Robert J.

Subjects
Biochemistry -- Research, Heparin -- Physiological aspects, Apolipoproteins -- Physiological aspects, Oligosaccharides -- Physiological aspects, Enzymes -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the apolipoprotein E, a lipid-transport protein in human plasma and brain. The interactions of the N-terminal domain of this apolipoprotein with enzymatically prepared heparin oligosaccharide have been explored.

Published
2001

2. Interaction of phospholipase A2 with thioether amide containing phospholipid analogues

Author

Plesniak, Leigh A., Boegeman, Scott C., Segelke, Brent W., and Dennis, Edward A.

Subjects
Poisonous snakes -- Venom, Phospholipases, Phospholipids -- Research, Biological sciences, Chemistry
Abstract

The use of transferred nuclear Overhauser enhancement (NOE) experiments to determine the conformation of two substrate analogues when bound to the cobra venom phospholipase A2 (PLA2) was reported. Both 1-thioether 2-amide phosphoethanolamine and the corresponding phosphocholine analogue adopt a PLA2-bound conformation in which the end of the sn-2 chain is within 5 angstrom of the alpha-methylene of the sn-1 chain. Moreover, intermolecular contact points between the inhibitor and the enzyme were identified by NOEs.

Published
1993

3. Different apolipoproteins impact nanolipoprotein particle formation

Author

Chromy, Brett A., Arroyo, Erin, Blanchette, Craig D., Bench, Graham, Benner, Henry, Cappuccio, Jenny A., Coleman, Matthew A., Henderson, Paul T., Hinz, Angie K., Kuhn, Edward A.;, Pesavento, Joseph B., Hoeprich, Paul D., Segelke, Brent W., Sulchek, Todd A., Tarasow, Ted, and Walsworth, Vicki L.

Subjects
Apolipoproteins -- Chemical properties, Atomic force microscopy -- Technology application, Nanotechnology -- Research, Phospholipids -- Research, Transmission electron microscopes -- Usage, Technology application, Chemistry
Abstract

The formation of different sized nanoliprotein particles (NLPs) by the interactions between apolipoproteins and phospholipids is discussed. The selection of apolipoprotein used in an assembly causes the size and homogenity of the final nanostructure.

Published
2007

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