Abstract
The structures of the filamentous bacteriophage f1 and its gene 3 amber mutant R4 have been compared using electric birefringence, electric dichroism, and ultrasonic vibration. The electro-optic experiments showed that the phage particles can be oriented in an electric field. The birefringence and dichroism as a function of field strength are not the same for the A-protein mutant and for the wild-type particle. Studies using ultrasonic vibration to fragment the bacteriophage show that the stabilities of the f1 and R4 particles differ. We have interpreted the structural differences between the particles as reflecting alterations in the arrangement of the subunits of the major capsid protein, the B-protein; further, the observed suppressor dependence indicates that the subunit packing is controlled by the A-protein. Models for the mechanism of A-protein function are discussed.
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