Barrier-free paths of directed protein motion in the erythrocyte plasma membrane.
AUTOR(ES)
Boal, D H
RESUMO
A model is presented for the steric interaction between a plasma membrane protein and the membrane cytoskeleton in the human erythrocyte. The cytoskeleton is treated as a network of polymer chains attached to a flat bilayer, and the membrane protein is a hemisphere of effective radius R(e) with center on the bilayer edge. The simulation is used to investigate the barrier-free path L for linear guided motion of a protein in the bilayer plane. It is shown that the barrier-free paths of small proteins can be used to extract the effective in-plane diameter of cytoskeletal components. For example, the in-plane diameter of an ankyrin attachment site is found to be approximately 12 nm in the simulation, or twice the computational spectrin diameter. The barrier-free paths of large proteins (R(e) > 23 nm) vanish when the proteins are corralled by the cytoskeleton. For intermediate size proteins, L decreases approximately as L is directly proportional to S-1.4 where S is proportional to the sum of the protein and cytoskeleton chain radii.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1236261Documentos Relacionados
- Myotonic muscular dystrophy: defective phospholipid metabolism in the erythrocyte plasma membrane.
- Plasmodium falciparum polypeptides associated with the infected erythrocyte plasma membrane.
- Syndeins: the spectrin-binding protein(s) of the human erythrocyte membrane.
- Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane.
- Protein 4.1: its association with the human erythrocyte membrane.
