Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.

doi:10.1016/s0014-5793(98)00876-x

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Article

Unfolding of bacteriophage P22 tailspike protein: enhanced thermal stability of an N-terminal fusion mutant.

FEBS letters - 7 Aug 1998

Carbonell X, Villaverde A

Abstract excerpt

The tailspike protein (TSP) of bacteriophage P22 is a homotrimeric multifunctional protein responsible for cell attachment and hydrolysis of the Salmonella typhimurium host cell receptor. Despite the folding of TSP involves the formation of thermolabile intermediates, the mature protein is extrem...

Topics

Bacteriophage P22
Glycoside Hydrolases
Kinetics
Mutagenesis, Insertional
Mutation
Protein Conformation
Protein Folding
Recombinant Fusion Proteins
Temperature
Viral Proteins
Viral Tail Proteins

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