Molecular motion and association on the cell surface.
The size, shape, flexibility and topological relationships of proteins and lipids on cell surfaces and in artificial membranes have been studied by: (1) rotational and translation diffusion using time-resolved spectroscopy of singlet and triplet probes, and (2) fluorescence energy transfer in a flow system.
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000378:metabolism; D066246:ErbB Receptors; D005399:Fishes; D006183:H-2 Antigens / Q000276:immunology; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D008954:Models, Biological; D008968:Molecular Conformation; D011940:Receptor Aggregation; D011956:Receptors, Cell Surface / Q000378:metabolism; D011950:Receptors, Cholinergic / Q000378:metabolism
D006183:H-2 Antigens; C024755:H-2K(K) antigen; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic; D004815:Epidermal Growth Factor; D066246:ErbB Receptors