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

doi:10.1006/jmbi.1998.1944

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Article

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

Journal of molecular biology - 14 Aug 1998

Schuler B, Seckler R

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...

Topics

Bacteriophage P22
Glycoside Hydrolases
Mutation
Protein Folding
Protein Structure, Secondary
Thermodynamics
Viral Tail Proteins

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