Bacteriophages mutant

Lysozyme from bacteriophage T4 is a 164 amino acid polypeptide chain that folds into two domains (Figure 17.3) There are no disulfide bridges the two cysteine residues in the amino acid sequence, Cys 54 and Cys 97, are far apart in the folded structure. The stability of both the wild-type and mutant proteins is expressed as the melting temperature, Tm, which is the temperature at which 50% of the enzyme is inactivated during reversible beat denat-uration. For the wild-type T4 lysozyme the Tm is 41.9 °C. 

FIG. 1 Monolayer of T7 phage heads. Cryoelectron micrograph of tailless mutant of T7 bacteriophage. Bar 50 nm. (From Ref. 42. Copyright 1997 Cell Press.)... 

The rotational dynamics of ethidium intercalated in double-strand DNAs of intact bacteriophages, namely, X, the deletion mutant XA, T4D (wild type), and T4dC (with normal cytosine instead of glucosylated hydroxymethyl-... 

Escherichia coli (strain 201 infected with bacteriophage T4amBL292, a maturation defective phage mutant, host-coded activity which is a component of T4 dNTP-synthesizing enzyme complex [2]) [2]... 

Katsura I, Structure and function of the major tail protein of bacteriophage lambda, Mutants having small major tail protein molecules in their virion, J. Mol. Biol., 146 493-512, 1981. 

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