Interaction of deoxycholate and of detergents with the coat protein of bacteriophage f1.
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.
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
D003902:Detergents; D013501:Surface-Active Agents; D014764:Viral Proteins; D003840:Deoxycholic Acid; D012967:Sodium Dodecyl Sulfate