This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Proteins from the BAR domain superfamily [1], ubiquitous in many organisms and cell types (www.ks.uiuc.edu/Research/BAR-domain), are implicated in a multitude of cellular processes involving membrane remodeling, e.g., endocytosis, apoptosis, and cell-cell fusion. In vitro, these proteins sculpt high-curvature membrane tubes and vesicles [2, 3] from low-curvature liposomes. BAR domains form banana-shaped homodimers bearing a high density of positively charged residues on the concave surface [4?6], which facilitates sculpting of negatively charged membranes. However, single BAR domains induce only local membrane curvature [7, 8], while recent cryo-EM reconstructions [3] reveal that sculpting of membrane tubes and vesicles is performed by many BAR domains arranged in lattice-like scaffolds.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR005969-21
Application #
8172043
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2010-08-01
Project End
2011-07-31
Budget Start
2010-08-01
Budget End
2011-07-31
Support Year
21
Fiscal Year
2010
Total Cost
$33,491
Indirect Cost
Name
University of Illinois Urbana-Champaign
Department
Type
Organized Research Units
DUNS #
041544081
City
Champaign
State
IL
Country
United States
Zip Code
61820
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Vermaas, Josh V; Taguchi, Alexander T; Dikanov, Sergei A et al. (2015) Redox potential tuning through differential quinone binding in the photosynthetic reaction center of Rhodobacter sphaeroides. Biochemistry 54:2104-16
Belkin, Maxim; Chao, Shu-Han; Jonsson, Magnus P et al. (2015) Plasmonic Nanopores for Trapping, Controlling Displacement, and Sequencing of DNA. ACS Nano 9:10598-611
Shen, Rong; Han, Wei; Fiorin, Giacomo et al. (2015) Structural Refinement of Proteins by Restrained Molecular Dynamics Simulations with Non-interacting Molecular Fragments. PLoS Comput Biol 11:e1004368

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