title: Interaction of deoxycholate and of detergents with the coat protein of bacteriophage f1.
abstract: The major coat protein of bacteriophage f1, which is localized in the host membrane during phage maturation, has a hydrophobic binding site capable of binding deoxycholate and a variety of detergents to form a soluble particle, and in that respect, resembles many membrane proteins. The soluble particle has properties that suggest it is formed by simple insertion of protein into a deoxycholate or detergent micelle, but molecular weight measurements show that the protein is present as a dimer, even in sodium dodecyl sulfate, indicating the existence of unusually strong forces for self-association. A by-product of the investigation has been to show that detergents can be very helpful in the fractionation of the constituent molecules of the virus: deoxycholate-solubilized virus is readily fractionated by gel chromatography into DNA, A protein, and B protein, with virtually no cross-contamination.
mesh_terms: D001665:Binding Sites; D002850:Chromatography, Gel; D002942:Circular Dichroism; D003090:Coliphages; D004267:DNA Viruses; D003840:Deoxycholic Acid; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli; D011485:Protein Binding; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate; D013501:Surface-Active Agents; D014764:Viral Proteins / Q000302:isolation & purification
chemical_list: D003902:Detergents; D013501:Surface-Active Agents; D014764:Viral Proteins; D003840:Deoxycholic Acid; D012967:Sodium Dodecyl Sulfate