Ms. Cameron A Haase-Pettingell

Cameron Haase-Pettingell is involved in the studies of the Salmonella phage P22 tailspike as an example of folding and aggregation. The tailspike is a site of a number of types of mutations that effect the folding and aggregation of the tailspike chains. The mutation types in the tailspike are:

(*) temperature sensitive for folding (tsf),
(*) global suppressor of folding (su),
(*) cold sensitive (cs),
(*) Cys>Ser to study the transited disulfides,
(*) mutations that accumulate monomeric or trimeric intermediates in the folding pathway, and
(*) mutations that in the hydrophobic core of the tailspike.

These can be studied by examining the in vivo folding and in vitro refolding at permissive and restrictive temperatures. We can assess activity of the tailspike protein by examining head binding, cell killing and thermal melting, allowing us to determine the effect these mutations have on folding and aggregation and giving a better picture of the effect amino acid environment direct the folding of a protein.