The shape of spectrin molecules from human erythrocyte membranes.
Purified spectrin dimers and tetramers have been directly visualized by low-angle shadowing. The 9-S heterodimer is an asymmetric flexible molecule about 1000 A in length, its constituent monomer polypeptides forming two strands which in many molecules are individually visible, lying partially separated from one another or twisting round each other in a loose double helix. The 12-S tetramer is formed by the end-to-end association of two heterodimers, without overlap. The protein bears no physical resemblance to myosin.
D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D004912:Erythrocytes / Q000648:ultrastructure*; D006801:Humans; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008854:Microscopy, Electron; D009218:Myosins; D011487:Protein Conformation; D013049:Spectrin
D046911:Macromolecular Substances; D008565:Membrane Proteins; D013049:Spectrin; D009218:Myosins