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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yin, Ying Arkhipov, Anton Schulten, Klaus |
| Description | Country affiliation: United States Author Affiliation: Yin Y ( Department of Physics and Beckman Institute, University of Illinois at Urbana-Champaign, 405 North Mathews, Urbana, IL 61801, USA.) |
| Abstract | Membrane compartments of manifold shapes are found in cells, often sculpted by cellular proteins. In particular, proteins of the BAR domain superfamily participate in membrane-sculpting processes in vivo and reshape also in vitro low-curvature membrane liposomes into high-curvature tubes and vesicles. Here we show by means of computer simulations totaling over 1 millisecond, how lattices involving parallel rows of amphiphysin N-BAR domains sculpt flat membranes into tubes. A highly detailed, dynamic picture of the 100-microsecond formation of membrane tubes by lattices of N-BAR domains is obtained. Lattice types inducing a wide range of membrane curvatures, with radii approximately 15-100 nm, are explored. The results suggest that multiple lattice types are viable for efficient membrane bending. |
| File Format | HTM / HTML |
| ISSN | 09692126 |
| e-ISSN | 18784186 |
| DOI | 10.1016/j.str.2009.03.016 |
| Journal | Structure |
| Issue Number | 6 |
| Volume Number | 17 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2009-06-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Molecular Biology Discipline Biochemistry Discipline Biotechnology Cell Membrane Metabolism Cellular Structures Computer Simulation Nerve Tissue Proteins Lipid Bilayers Liposomes Membrane Fluidity Membrane Proteins Models, Chemical Models, Molecular Protein Binding Protein Structure, Tertiary Proteins Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology |
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