P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.

Abstract excerpt

The folding of the trimeric phage P22 tailspike protein is influenced by amino acid substitutions of two types, virtually all of which affect residues in the central domain, a large parallel beta-helix. Temperature sensitive folding (tsf) mutations lead to drastically decreased folding yields at elevated temperature. Their phenotype can be alleviated by global suppressor (su) mutations. Both types of mutations...

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