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Search Publications by: Frank Heinrich (Assoc)

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Displaying 26 - 50 of 72

Fast Formation of Low-Defect-Density Tethered Bilayers by Fusion of Multilamellar Vesicles

January 10, 2017
Author(s)
Tadas Ragaliauskas, Mindaugas Mickevicius, Bozena Rakovska, Tadas Penkauskas, Frank Heinrich, Gintaras Valincius
Multilamelar vesicles fuse to molecular-anchor-grafted surfaces yielding low defect density, tethered bilayer membranes. Continuous bilayers are formed within 10 min, while the electrically insulating bilayers with less than 0,1 υmu-1} defect density can

Segmental Deuteration of a-Synuclein for Neutron Reflectometry on Tethered Bilayers

January 5, 2017
Author(s)
Zhiping Jiang, Frank Heinrich, Ryan P. McGlinchey, James M. Gruschus, Jennifer C. Lee
Neutron reflectometry (NR) is uniquely suited for studying protein interaction with phospholipid bilayers. While molecular details along the bilayer normal can be obtained on an Angstrom scale, NR cannot discern specific membrane-bound protein regions due

HIV-1 Matrix-31 Membrane Binding Peptide Interacts Differently with Membranes Containing PS vs. PI(4,5)P 2

September 15, 2016
Author(s)
Lauren O'Neil, Kathryn Andenoro, Isabella Pagano, Laura Carroll, Leah Langer, Zachary Dell, Davina Perera, Bradley W. Treece, Frank Heinrich, Mathias Loesche, John F. Nagle, Stephanie Tristram-Nagle
Efficient assembly of HIV-1 at the plasma membrane (PM) of the T-cell specifically requires PI(4,5)P 2. It was previously shown that a highly basic region (HBR) of the matric protein (MA) on the Gag precursor polyprotein Pr55^gag^ is required membrane

Membrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation

May 1, 2016
Author(s)
Marilia Barros, Frank Heinrich, Siddhartha A. K. Datta, Alan Rein, Ioannis Karageorgos, Hirsh Nanda, Mathias Loesche
Retroviral Gag polyprotein is the structural determinant that assembles in a protein lattice on the host's plasma membrane to trigger formation of the viral protein/membrane shell. In this process, it employs multiple signals - electrostatic, hydrophobic

A Bacteriophage Endolysin that Eliminates Intracellular Streptococci

March 15, 2016
Author(s)
Yang Shen, Marilia Barros, Tarek Vennemann, David Travis Gallagher, Yizhou Yin, Sara B. Linden, Ryan D. Heselpoth, Dennis J. Spencer, David M. Donovan, John Moult, Vincent A. Fischetti, Frank Heinrich, Mathias Loesche, Daniel C. Nelson
PlyC, a bacteriophage-encoded A-B endolysin, lyses Streptococcus pyogenes (Spy) on contact and protects mice from upper respiratory Spy colonization. Here, we demonstrate that PlyC is a novel, potent agent for targeting and controlling intracellular Spy

The PTEN Tumor Suppressor Forms Homodimers in Solution

August 21, 2015
Author(s)
Frank Heinrich, Srinivas Chakravarthy, Hirsh Nanda, Antonella Papa, Pier Paolo Pandolfi, Alonzo H. Ross, Rakesh K. Harishchandra, Arne Gericke, Peter M. Loesche
The PTEN tumor suppressor exerts phosphatase activity on PI(3,4,5)P 3 in the plasma membrane and was recently reported to dimerize in cell models. Here we show that PTEN forms homodimers in vitro and determine a structural model of the complex from SAXS

Deuteration in Biological Neutron Reflectometry

June 30, 2015
Author(s)
Frank N. Heinrich
Neutron reflectometry is uniquely positioned in structural biology, because of its ability to characterize biomimetic interfacial architectures like lipid membranes and membrane-associated proteins non-destructively and in their native environment

Structural Features of Membrane-bound Glucocerebrosidase and a-Synuclein Probed by Neutron Reflectometry and Fluorescence Spectroscopy

January 9, 2015
Author(s)
Thai Leong Yap, Zhiping Jiang, Frank Heinrich, James M. Gruschus, Candace M. Pfefferkorn, Marilia Barros, Joseph E. Curtis, Ellen Sidransky, Jennifer C. Lee
Mutations in glucocerebrosidase (GCase), the enzyme deficient in Gaucher disease, are a common genetic risk factor for the development of Parkinson disease (PD) and related disorders, implicating the role of this lysosomal hydrolase in the disease etiology

Structure and Stability of Phospholipid Bilayers Hydrated by a Room-Temperature Ionic Liquid/Water Solution: a Neutron Reflectometry Study

October 23, 2014
Author(s)
Antonio Benedetto, Frank Heinrich, Miguel A. Gonzalez, Giovanna Fragneto, Erik Watkins, Pietro Ballone
Neutron reflectometry measurements (NR) have been carried out to probe the structure and stability of two model bio-membranes consisting of POPC and DMPC phospholipid bilayers hydrated by water solutions of two prototypical room-temperature ionic liquids